01 ScienceOfMacros

DE F I N IT IIVE
DEFINIT GUIDE
VE GU IDE
THE SCIENCE
AND PRACTICE
OF MACROS
UNIT 1
The science of
macronutrients
1
In this Unit:
• We’ll provide an introduction to the science of

macronutrients and energy, including:
• What are macronutrients?
• What is a macronutrient ratio, or split?
• What’s the role of energy (i.e., calories) and energy

balance?
• For each group of macronutrients, we’ll explain:
• their structure and function;
• similarities and differences among the molecules in each

group; and
• what those nutrients do in our bodies.
• We’ll show how knowing the nutritional science helps us

understand why we might choose particular foods and
nutrients for particular goals.
PN DEFINITIVE GUIDE: The science and practice of macros
Introduction
and orientation
We eat to get energy and nutrients for life.
Life is a dynamic, ever-changing set of reactions and interactions between
biological systems.
• We need energy to supply the power for physiological processes.
• We need nutrients to make up the chemical components and building blocks
of those processes.
How much (or how little) energy we take in or expend, and what nutrients we
eat in what amounts, can fundamentally affect how our bodies work.
This concept is the basis for organizing a nutritional plan around “macros”, or
macronutrients.
1. Both the quantity that we eat (i.e., our energy intake) and the quality that we
eat (i.e., the nutrient makeup of our foods) can affect physiological function.
2. This, in turn, affects our health, performance, recovery, and body weight or
body composition (i.e., how much lean or fat mass we have).
A good macro-based plan helps people:
• eat the right amount of food for their goals and needs;
• optimize the contribution of each macronutrient; and
• choose high-quality, nutrient-rich foods.
UNIT 1: The science of macronutrients | 2

What are macronutrients?

Macronutrients — from the ancient Greek makros, or “large” — are large, MACRONUTRIENTS
Large families of nutrients
diverse families of molecules that make up the food we eat, and which we can
(mainly proteins,
divide into three main groups: carbohydrates, and fats) that
1. Proteins. make up the bulk of the food
we eat and provide energy
2. Carbohydrates.
3. Fats.
Each of these macronutrients contains energy (which, in North America, we CALORIES
usually measure in calories), as well as smaller components that can be broken A measure of energy stored
down and used individually. in food
For instance:
• Proteins can be broken down into various amino acids. AMINO ACIDS
Building blocks of protein
• Carbohydrates can be broken down into various sugars (aka saccharides)
or, in the case of indigestible fiber, barely broken down at all (but perhaps
enjoyed by our gut bacteria, and converted into other substances).
SACCHARIDES
• Fats can be broken down into various fatty acids. Building blocks of
carbohydrates such as
While each food has a different macronutrient composition, as well as a sugars and starches
different amount of available energy, all foods are made of at least one
macronutrient.
(Alcohol, by the way, is considered a fourth macronutrient, because we can FATTY ACIDS
use it for energy. We’ll touch on it a bit, but since hopefully you aren’t making Building blocks of lipids
alcohol a major part of your intake, we won’t talk about it too much.) (fats)
While macronutrients are important, they aren’t the only factors

to consider in nutritional plans.
Foods aren’t just a lump of molecules that we can surgically dissect into their
chemical components.
In part, this is because:
• Most foods are a mix of macronutrients, and subtypes of macronutrients. For
instance, a nut might contain fat, protein, and carbohydrates (mainly in the
form of fiber). And, the fat that nut contains isn’t just one kind of fat — there
may be several types of fatty acids in it, all with different jobs in the body.

• Macronutrients vary a lot in their makeup. For instance, the family

of “carbohydrates” includes everything from the simplest sugars (such
as glucose or fructose) to the most complex fibers (such as cellulose).
Differences between types of macronutrient molecules affect how our bodies
digest, absorb, and use them. So all proteins, carbohydrates, and fats are
not created equal!
• Foods have many other components, such as water or micronutrients (e.g.,
vitamins, minerals, and other chemical compounds).
• We eat meals, not just foods. Meals involve dozens, perhaps hundreds of
molecules and nutrients integrated into something that creates a flavor, a
texture, and a holistic sensory or digestive experience.
In other words:
Macronutrients matter, but meals are much more than the sum of their parts.
We’ll look at this more later.
What is a macronutrient ratio?

When we talk about a macronutrient ratio (or use a phrase like “hitting MACRONUTRIENT RATIO
How much energy each
your macros”), we’re talking about how much energy and nutrition each
macronutrient contributes to
macronutrient contributes in the context of a whole diet. total energy intake
We generally express this in terms of percentages. For instance, a typical
“balanced” or mixed meal might include:
• 30% of total energy coming from protein;
• 40% from carbohydrates; and
• 30% from fat.
chicken thighs
30% Protein
brown
rice
apple
40% Carb
avocado
FIGURE 1
30% Fat asparagus
A “balanced”
or mixed meal

We might also set numeric targets in the form of grams. For instance, most
athletes may want to make sure they eat enough carbohydrates and protein, so
they may also track how many grams they’re getting of each.
Key points:
• Each macronutrient has different roles in our bodies.
• Eating different amounts of protein, carbohydrates, and fats will have
different effects in our bodies.
• Changing the macronutrient ratio will change our physiological outcome.
For instance:
• If we don’t get enough protein, our bodies won’t repair or recover
themselves.
• But, if we eat only protein without enough carbohydrate or fat, we can end
up starving to death because our bodies also need carbohydrates and fat for
other crucial metabolic processes.
The reason to learn about macros, then, is:
To discover the energy intake as well as the optimal ratio of protein,
carbohydrate, and fat that will help you (or your clients) look, operate,
perform, and recover as well as possible.
How general or specific you get with this will depend on your (or your clients’)
individual needs and goals. (We’ll look at how to apply this later.)
Although there are some broad guidelines, each person will differ in the specific
macronutrient ratio that makes them feel and function best.
Food quality also matters.

• Just looking at how much protein, carbohydrate, and/or fat we may be
eating doesn’t tell us the full story.
• Each macronutrient group contains a wide variety of molecules with
different chemical and physical structures.
• The chemical and physical structure of those diverse molecules affects
how they behave in our bodies.
For example:
• One type of fat may increase inflammation, while another type may decrease it.
• One type of carbohydrate may be quickly digested and absorbed, while
another type may not be digested nor absorbed at all.

Again, macronutrients are not a single type of molecule, but rather large groups
or families of molecules that individually have different jobs.
Just looking at the macronutrient profile of a diet (i.e., the percentage or total
grams of proteins, fats, and carbohydrates) does not tell us:
• what types of macronutrient molecules are in it; nor
• the quality of that diet.
What is the role of energy?

Key points:
• We take in energy in the form of food. (Or, we can retrieve previously
stored food energy from our body’s tissues, such as our fat or muscle tissue.)
• We expend energy to stay alive (i.e., metabolism), to stay warm, to repair
tissues, to replenish stored fuel, and to move.
• This relationship between energy in and energy out is known as energy ENERGY BALANCE
balance. The relationship between
energy in from food and
• Energy balance is a key element to consider when planning a macro- energy out from metabolic
based nutrition program. activity and movement
Energy balance strongly affects our health, body composition,

and performance.
Energy balance determines our body weight.
• If we take in more energy than we use or excrete, we gain weight.
• If we take in less energy than we use or excrete, we lose weight.
• If we take in the same amount of energy than we use or excrete, we stay
the same.
This is true regardless of the macronutrient composition of our diets, our
specific food choices, what time of day we eat, or any other details of our
nutritional plan.
This basic relationship is simple.
But that doesn’t mean what occurs in between “energy in” and “energy out”
is simple.

Energy in
Calories Energy out
eaten Calories
burned
Energy balance
Maintain weight
out
Energy s
C a lo r ie
in
Energy burned
s
Calorie
e a te n
Energy excess
Gain weight
Energy
in
Calorie
s
eaten
Energy
ou
Calorie t
s
burned
Energy deficit
Lose weight
Or that energy balance is easy to change. (After all, if it was easy to change, FIGURE 2
we’d all be out of coaching jobs.) Energy balance
Many factors can affect energy balance, and consequently the results we get.
For more on this, see our articles:
Calories In vs. Out? Or Hormones? The Debate Is Finally Over.
The Surprising Problem with Calorie Counting Part 1: Calories In
The Surprising Problem with Calorie Counting Part 2: Calories Out

Factors that influence Factors that influence

“energy in” “energy out”
Appetite Energy burned at rest

Influenced by hormones that regulate Influenced by body size, hormones,
appetite and satiety dieting history, genetic factors, health,
Food consumed sleep quality, age
Influenced by availability, palatability, Energy burned through exercise
energy density, sleep quality, education, Influenced by exercise ability, intensity,
socioeconomic status, culture duration, frequency, and environment,
Calories absorbed as well as hormones and sleep quality
Influenced by macronutrient intake, Energy burned through non-exercise activity
food prep, age, microbiome, health, Influenced by health, energy status, stress,
energy status hormones, occupation, leisure activities,
Psychological factors genetic factors
Influenced by stress levels, mindset, Energy burned by metabolizing food
perceived control, self-esteem, Influenced by macronutrient makeup and how
sleep quality processed the food is
Moreover, while energy balance determines body weight, it doesn’t tell us much FIGURE 3
about body composition, i.e., the ratio of lean mass (such as muscle and Factors that can affect
energy balance
bone) to fat mass.
Body composition is influenced by factors such as our:
• hormones (such as testosterone, estrogen, or growth hormone);
• exercise (e.g., how often, how intensely, how long, what type of exercise, BODY COMPOSITION
and so on); The ratio of lean mass (such

as muscle and bone) to fat
• age; mass
• medication use;
• genetic predisposition; and, of course,
• macronutrient intake (especially protein).

Energy balance can also affect physiological function, performance,

and recovery.
Beyond just gaining or losing weight, energy balance can affect many other
biological systems.
For example:
• Hormonal health and balance can be disrupted by either too much or too
little energy, especially over a long period of time.
• If we don’t eat enough energy, our physical and mental performance may
decline.
• People recovering from surgery or major injuries (such as broken bones) may
need more energy than healthy people, as energy is going to tissue repair
and rebuilding.
Because energy balance is so important physiologically, our bodies have

systems in place to regulate it.
We have sensors and complex feedback loops throughout our bodies that tell
our brains (particularly our hypothalamus, aka Mission Control) how much HYPOTHALAMUS
energy is available. A central regulator in our
brain of many physiological
Our brains can then respond by adjusting the dynamics of these biological functions, such as
systems, to either maintain balance or try to make changes. metabolism
For instance:
• If energy intake is consistently too low for a person’s needs, that person
may eventually start to struggle with hunger, appetite, and food cravings.
They may also feel cold or have sluggish digestion. Their bodies are slowing
metabolic rate and increasing the desire to eat, in order to compensate.
• If energy intake is consistently too high for a person’s needs, that person
will likely store the extra energy as fat. However, depending on the person,
excess energy can also be used for recovery, repair, and growth (for instance,
in building muscle); or thrown off as heat. They may also want to eat less or
move more, in order to compensate.
Some macronutrients, or types of foods, are more satiating than others.
For instance:
• A high-protein, high-fat, and/or high-fiber diet tends to make people feel
fuller, and consequently eat less.

• Diets high in processed foods (such as pastries, sweets, cereal, pizza, etc.)
tend to make people eat more, and feel less satisfied.
This means:
When planning a macronutrient-based program:

Consider how much energy you (or your clients) will need in order to:
• move towards body weight or body composition goals; and
• support physical activity, recovery, and/or metabolic health.
We’ll look at specific recommendations more in Unit 3. (And, if you’d like
an even deeper dive into nutritional science and coaching, see our Level 1
Certification.)
Each macronutrient stores a different amount of energy.

We measure food energy in either calories or joules.
Calories are a measure of heat, while joules (J) are a measure of work. Both JOULES
of these are ways to describe how much energy might be stored in food, or A measure of energy, work
or amount of heat. Is used
released through energy expenditure (or excretion).
for measuring food energy.
Calories (which are actually kilocalories, or kcal) or joules (kilojoules, or kJ) are 4.184kJ = 1 kcal
listed on your food labels, depending where you live. You might also see energy
expenditure described in watts (for example, on an exercise machine), which is WATTS
equal to 1 J/s. A measure of power output;
energy per unit time
(International Units are
Joule/second)

Regardless of how energy is measured, what matters most is:

• There is an important relationship between energy going in to the body,
and energy stored, used, and excreted by the body.
• Different macronutrients and types of food contain and release different
amounts of energy.
Here are some examples of the energy (in calories) released from particular
molecules when burned in a lab, using a specialized instrument known as a
bomb calorimeter. BOMB CALORIMETER
A lab tool that measures the
• 1 gram of fat = 9.44 kcal heat energy produced from
• 1 gram of starch = 4.18 kcal combusting a food, and thus
how many calories that food
• 1 gram of sucrose or glucose = 3.94 kcal contains
• 1 gram of protein = 5.65 kcal

• 1 gram of alcohol = 7.09 kcal
However, human bodies are not lab instruments. Food we eat isn’t just
“burned” for heat. Rather, it must be consumed, broken down, digested,
absorbed, transported to various locations, and incorporated into a vast array of
chemical reactions.
This means:
Each macronutrient molecule type releases different amounts of energy to us
when we break it down in the process of digestion and absorption.
For instance, although carbohydrates have approximately 4 calories (kcal) of
energy per gram:
• We’ll absorb almost all of the energy in 100 calories of table sugar, because
it breaks down quickly and easily in our bodies.
• We’ll absorb less of the energy in 100 calories of brown rice, because some
of it is fiber that will be partially bound to waste products and excreted.
• We’ll absorb none of the energy in 100 calories of tree bark, although we
can see that stored energy if we actually do burn it for heat!
While all of these are technically “carbohydrates”, their effects in our bodies are
quite different.

In the real world, calculating energy needs, intake, and use is

more of an art than a science.
While we can make an educated guess at how much energy a person
might need or expend, it’s only ever a guess.
Outside of a lab:
• We can’t know exactly how many calories and nutrients we absorb, use,
and/or excrete.
• We can’t know exactly how many calories and nutrients are in our food.
• We can’t know exactly how many calories and nutrients we expend through
metabolism and movement.
Thus:
Precise, meticulous, highly detailed calorie counting as a way to manage diet
and exercise is time consuming, tedious, and unnecessary for most people.
Instead, we can start with predictive equations to estimate how much energy PREDICTIVE EQUATIONS
the body needs or uses, based on several factors such as sex, age, height, Formulae that account for
weight, and activity level. (We’ll look more at predictive equations in Unit 2.) various factors such as sex,
age, height, and weight to
As their name suggests, these equations are just predictions, or guesses. estimate metabolic rate
They’re based on population averages, which means they might not hold up for
people who fall outside an “average” range (such as people who are much bigger
or smaller, people who are extremely active, and so on). Even if we’re extremely
careful and precise with our measures, and even if the person we’re measuring
falls neatly into the average, there’s still at least a 5% margin of error.
We also cannot know exactly how someone’s body may change.
While it’s often cited, for instance, that we’ll lose 1 lb (0.45 kg) for every 3500
calories of deficit, in actual physiological systems (i.e., our bodies), it doesn’t
work that way. Body change is complex, nonlinear, and often surprising.
For example, if we take a hypothetical person — let’s say a sedentary 220 lb
(100 kg) man who wants to lose weight — and feed him exactly 480 kcal less
per day (so, nearly 3500 calories/week less) and track his progress over 10
years, his weight change graph would look like this:

100 Predicted bodyweight

Expected inter-individual variability
95
90
85
Bodyweight (kg)
80
75
70
65
60
0
2 4 6 8 10
Time (years)
As you can see: FIGURE 4

Predicted body weight plus
• He doesn’t keep losing weight forever, nor is it a straight line downwards. possible variation over time
• There’s a significant range of variation in how much weight he could lose.
• In real life, his weight loss could vary by around 10-12 kg (22-26 lb) over
time. So, his weight might level out anywhere between around 72-82 kg
(159-181 lb).
Over time, as we gather data about our (or our clients’) progress, we can adjust
energy balance and nutrient intake based on the objectively measured results
we’re getting.
In other words: Follow reality rather than rules.

Try it now.
We’ll look more at tailored energy and macronutrient calculations

using the PN Professional Nutritional Calculator in Unit 2.
If you want to get started with trying something, here’s a link to the
Precision Nutrition Weight Loss Calculator, which uses a predictive
equation and a research database to estimate how much energy it
might take you to lose, gain, and/or maintain your weight.
Since this equation is just a prediction, depending on the person, the
calculations may be off by as much as 15%. (And this is currently
the best model available!)
Try playing with different inputs and the Advanced Controls to see
how it affects the output.

Protein
What are proteins?
Proteins are crucial physiological molecules.
They’re the most abundant macromolecule (“large molecule”) in biology, and MACROMOLECULE
they’re involved in nearly every process that happens in our bodies. A large molecule; biological
macromolecules include
Such as: proteins, carbohydrates,
lipids, and nucleic acids
• cellular metabolism;
(DNA for example)
• sending messages within and between cells; and
• creating structures (such as tissues).
There are thousands of different types of proteins in every single cell, with
thousands of functions. This makes proteins vastly more complex and variable
than the other two macronutrients, carbohydrates and fats.
Our bodies are always building up and breaking down proteins.

This process is known as protein turnover. PROTEIN TURNOVER
The ongoing process of
Because proteins have many important jobs (as you can see in the list below),
breaking down and building
and because they’re always being deconstructed and reconstructed (with some up proteins in the body
inevitably lost in the process), we need to eat a consistent supply of dietary
protein to live and thrive.

Nutrition nerd stuff
The role of proteins • Inhibition of autophagy (cellular waste

removal and programmed self-destruction)
in our bodies and intracellular protein degradation
• Regulation of metabolism (activation of
the oxidation of glucose and long-chain
Or, “everything you’ve ever wanted to fatty acids to CO2 and water; inhibition of
know about the jobs that proteins do, but glucose and fatty acid synthesis)
were afraid to ask”.
• One-carbon unit metabolism and
Here’s a selection of the known biological methylation of DNA and proteins
roles of proteins and their component parts
of peptides and amino acids. • RNA and DNA synthesis, as well as amino
acid, heme, and carnitine synthesis
(Don’t worry, you don’t need to memorize this.)
• Activation of lipolysis and fat oxidation,
• Regulation of gene expression, as well as and reduction in white adipose (fat) tissue
micro-RNA biogenesis and levels
• Stimulation of brown adipose tissue
• Cell signaling via kinases (e.g., development and thermogenesis
mammalian target of rapamycin,
AMP-activated protein kinase, cGMP- • Appetite and body composition (e.g.,
dependent kinase, cAMP-dependent skeletal muscle, fat, and bone masses)
kinase, and mitogen-activated protein • Modulation of immune responses (T cell
kinase), G protein-coupled receptors, receptor, lymphocyte proliferation, the
and gaseous molecules (e.g., NO, CO production of cytokines and antibodies,
and H2S) macrophage polarization to affect the
• Nutrient transport and metabolism population of M1 and M2 cells, killing of
pathogens by NO, O2 −, and H2O2) and
• Transport of water, other amino acids and prevention of infectious disease (including
proteins, glucose, fatty acids, vitamins, viral infections)
and minerals
• Lactation (synthesis of amino acids,
• Major energy substrates for the small proteins, lipids, and carbohydrates by
intestine (glutamine, glutamate, and mammary glands)
aspartate) and immunocytes (glutamine)
• Reproduction (male and female fertility,
• Substrates for, and activation of, protein fetal growth and development, and
synthesis

possibly fetal programming of postnatal • Digestive function

metabolism and health)
• Chemical sensing via the G protein-
• Hormone secretion and endocrine status coupled receptors in the gastrointestinal
tract and possibly in other tissues
• Synthesis and secretion of hormones
(e.g., thyroid hormones, insulin, • Gastrointestinal emptying and the motility
glucagon, and glucocorticoids) of the small intestine
• Mediation of hormone actions • Conjugates with taurine and glycine to
facilitate lipid digestion and absorption
• Anti-oxidative defenses and removal of
toxic substances • Modulation of the growth, metabolism,
and population of the microbiota in the
• Synthesis of glutathione, carnosine,
lumen of the small intestine
creatine, and taurine
• Recovery from injury
• Synthesis of antioxidative enzymes (e.g.,
glutathione peroxidase, superoxide • Enhancement of wound healing after
dismutase and H2O2 peroxidase) surgery or injury (e.g., polyamine and NO
synthesis)
• Removal of ammonia and xenobiotics
• Synthesis of collagen and remodeling
• Anti-inflammation
of extracellular matrix (e.g., glycine and
• Regulation of apoptosis (programmed cell proline)
death) and aging
• Regulation of blood flow and cardiovascular
• Neurological function and behavior function (e.g., NO synthesis)
• Synthesis of neurotransmitters (e.g., • Other physiological processes
serotonin, γ-aminobutyrate, dopamine,
• Pigmentation (skin, hair, and eyes)
and acetylcholine)
• Regulation of acid–base balance (e.g.,
• Agonists and co-agonists of N-methyl-d-
renal ammoniagenesis from glutamine)
aspartic acid (e.g., glutamate, aspartate,
glycine, d-aspartate, d-alanine, and • Osmoregulation (e.g., taurine and
d-serine) glutamine in skeletal muscle, heart, and
fetal fluids)
• Neuroprotective reactions
Source: Wu G. Functional amino acids in nutrition and health. Amino Acids. 2013. pp. 407–411.

Amino acids PEPTIDES

Linked chains of amino acids
Proteins are made up of amino acids, and can range from simple to
AMINO ACIDS
complicated, small to large. The structure, shape, and makeup of proteins
Building blocks of protein
matters — there are thousands of proteins with a wide range of configurations,
all of which contribute to our physiological functioning.
AMINO
An amino acid is so named because it has an amino, or nitrogen group (with
A nitrogen-containing
the chemical formula NH2), on one end of its molecule, and an acidic carboxyl
chemical group in a
group (COOH) on the other. molecule
Amino acids also have what is called an “R group”, or side chain, which can
vary from amino acid to amino acid. Branched-chain amino acids (BCAAs) are R GROUP
so named because they have a branched side chain. Aka a side chain, a widely
varying structure making
up part of an amino acid
H molecule (as well as other

molecules)
H O BRANCHED-CHAIN AMINO
ACIDS (BCAAS)
N C C Amino acids with a branched
α-carbon side chain structure; this
group includes leucine,
H OH isoleucine, and valine
Amino group (NH2)

R Carboxyl group (COOH)
Side chain
You can think of amino acids, the units that make up proteins, as different FIGURE 5
colored Legos that can fit together in different ways. There are theoretically Basic protein molecule
endless ways that amino acids could create protein shapes and structures.
Protein synthesis is the building of new proteins. Following instructions from
PROTEIN SYNTHESIS
our DNA, proteins are built from amino acids into peptides; from peptides into
Building new proteins
polypeptides, and from there into increasingly complicated structures, some of
which can be incredibly intricate.
POLYPEPTIDES
This complex sequence, structure and shape determines what a specific protein
Chains of amino acids longer
does, much like a puzzle piece. For instance, one type of protein might become than 25 amino acids; also
an antibody; another might become a neurotransmitter. Within our body’s known as proteins

own structures, and within the foods we eat, most proteins are found in more ANTIBODY
complex forms. Immune signalling protein
that combats a specific
However, when we eat and digest complex proteins (say, in a steak or a piece of pathogen such as a virus
tofu), we break them down into smaller peptides and amino acids, and use those
amino acids to make new things, or for other metabolic functions in our bodies.
Protein synthesis
AA
AA
AA
AA
AA
AA
Peptide
Amino acids bond
AA
Polypeptides
Peptide (more complex structures
(chain of amino acids) of peptides)
Protein breakdown
Amino acids (and proteins) differ from carbohydrates and fats in their chemical FIGURE 6
structure because they contain nitrogen atoms. Nitrogen is about 16% of Protein turnover
dietary protein in terms of weight, making nitrogen metabolism an exclusive
and key part of protein metabolism. The presence of nitrogen in amino acids is
what helps us measure protein use and excretion, using an indicator known as NEUROTRANSMITTER
nitrogen balance (or the amount of nitrogen consumed versus excreted). Nervous system signalling
chemical
While in all of nature there are over 300 amino acids, in humans there are
20 proteinogenic, or protein-making, amino acids. The first, asparagine, was
discovered in 1808, and the last, threonine, was identified in 1938. NITROGEN BALANCE
Ratio between nitrogen
Amino acids mostly get their names from the food they were originally found consumed and excreted;
in. For instance, asparagine was first found in asparagus; glutamate in wheat a measure of protein
gluten; and tyrosine in cheese (tyrsos in Greek). Others got their name from adequacy in the body
some characteristic; for instance, glycine was named after sweetness (glykos in
Greek) because it tastes sweet. PROTEINOGENIC
Protein-making

Some scientists also include selenocysteine (an amino acid that has
selenium, discovered in 1991) and/or pyrrolysine (discovered in 2002), both
of which are present at very low levels in human proteins. Other amino acids
— ornithine, citrulline and homocysteine — have functions in the body, but
aren’t part of proteins.
Categorizing amino acids NON-ESSENTIAL AMINO

ACIDS
We can group amino acids based on their ability to dissolve in water. Non-polar Amino acids that our bodies
amino acids don’t dissolve well in water, while polar amino acids do. Polar can make
amino acids can be further categorized into the electrical charge they carry
(negative, positive, or no charge). These electrochemical configurations can
affect each amino acid’s behavior in our bodies. ESSENTIAL AMINO ACIDS
Amino acids that we must
For our purposes, it’s more useful to classify amino acids by their biological
get from our diet
roles, which are organized into three general categories:
• Non-essential amino acids: We can make these amino acids in our body, so
CONDITIONALLY
we don’t need to eat them in our diets (although, of course, we can).
ESSENTIAL AMINO ACIDS
• Essential amino acids: We need to get these essential amino acids (aka Amino acids that we may
EAAs) from food. We can’t make these ourselves. need to get from our diets in
special situations, such as
• Conditionally essential amino acids: We can make these amino acids illness
ourselves, but not always effectively, particularly when we’re under physical
stress (such as from hard athletic training, or when we’re sick). Having
extras around helps us rebuild tissues when those tissues are damaged.
Essential amino
FIGURE 7
acids (EAAs)
Types of amino acids
Lysine
Methionine Conditionally Non-essential
Phenylalanine essential amino acids 1
Notes: Histidine is a
Threonine amino acids Alanine special case, as it’s
Tryptophan Arginine Asparagine sometimes listed as an
Cysteine Aspartic acid essential amino acid.
Glutamine Glutamic acid However, unlike the other
Branched chain eight indispensable amino
Tyrosine Glycine
amino acids acids, it doesn’t reduce
Proline
(BCAAs) protein deposition and
Serine
Isoleucine induce negative nitrogen
Leucine Histidine
1 balance immediately when
Valine removed from the diet.
Proline is technically not
an amino acid.

This 3-part division of amino acids has been around for over 6 decades. It’s TRANSAMINATION
generally helpful, but the lines between categories are much more blurry than Transfer of an amino group
from one molecule to
most people realize.
another, particularly from an
Most people think of essential amino acids (EAAs) as amino acids that an amino acid to
a keto acid
organism can’t make at all, but that’s not true. In many cases, we can make
EAAs, but not enough for normal growth and survival. The processes that
produce these EAAs may be too slow to keep up with demands, or we may not
have enough of other substances that we need to make those EAAs.
For instance, we can actually make EAAs like the branched chain amino acids
(valine, isoleucine, and leucine) by using a process called transamination and α-KETO ACID
a particular molecule called an α-keto acid. With enough α-ketoisocaproic acid A particular type of keto
(KIC) around, your body can make leucine. acid, some of which are
involved in transamination
By the strictest definition of EAAs, only threonine and lysine are truly essential, reactions
in that there is no process by which mammals can make these amino acids.
Branched chain amino • a chemical signal (such as the presence

of particular amino acids or hormones
acids and muscle and peptides like insulin or IGF-1); and
protein synthesis • a mechanical signal (such as exercise).
Branched chain amino acids (BCAAs) are so The BCAA leucine has a special function in
named for their branched side chains, which muscle protein synthesis.
also happen to be essential amino acids. Leucine has its own transporter on the cell
For muscle protein synthesis to occur, there membrane, so it acts directly on the muscle
must be both: cells’ communication system (cell signaling)
to trigger protein synthesis. Leucine triggers

a series of cell signals to activate a protein — short-term protein synthesis maxes out
complex known as mTORC12 (mammalian/ after a meal containing about 10 g of EAAs,
mechanistic target of rapamycin complex or around 20-40 g of “real food” protein.
1) that then triggers the activation of
Cellular processes are extremely complex,
key protein regulators of muscle protein
so there’s always more to the story (and
synthesis (such as eukaryotic initiation
more proteins with more roles yet to be
factor 4E, eIF4E, which regulates DNA
discovered). For example, we recently
translation).
learned that mTORC1 can sense more
While BCAAs (particularly leucine) can amino acids than leucine, such as
stimulate muscle protein synthesis, on their glutamine and arginine levels.
own they’re not enough.
Muscle protein synthesis is much more
To get the most muscle protein synthesis, we complicated than any one amino acid.
need the other essential amino acids as well
2 Originally the protein within the complex was called mTOR (mammalian target of rapamycin), as this protein
responded to the addition of rapamycin to cell cultures. Today the name has been updated to mechanistic
target of rapamycin. Rapamycin (aka Sirolius) is an antibiotic used to suppress the immune system to stop
organ rejection after an organ transplant.
Stereoisomers: The same but different INSULIN

A hormone that helps
If you ever read a supplement label with specific amino acids you may have transport nutrients,
wondered why they all had an “L” in front of them — L-leucine, L-valine, particularly glucose,
L-threonine. What the heck is the “L” for? into cells
Many molecules, such as amino acids as well as sugars, exist as mirror images
IGF-1
of each other, like right and left hands. These molecular mirror images are
Aka insulin-like growth
called stereoisomers. factor 1, a hormone similar
to insulin that has anabolic
To differentiate between these mirror images, scientists use an L (or a minus
effects and promotes growth
sign) or D (or a plus sign).
• L stands for laevus (left in Latin).
CELL SIGNALING
• D stands for dexter (right in Latin). Cells’ communication
internally, or externally
with other cells and their
environment

TRANSLATION
The decoding of genetic
information from RNA
to protein
STEREOISOMERS
Molecules that are mirror
images of each other
However, unlike your hands, L and D molecules have different physiological FIGURE 8
effects. All amino acids that are important in nutrition are L-amino acids. This Sample supplement label
means that if you ate a ton of D-amino acids, you still would be deficient.
Many poor undergrads in chemistry have had to memorize rules on determining
whether a molecule is D or L, but we won’t go into that. What you need to know
is: All amino acids can have L- and D-isomers, with the exception of glycine, ISOMERS
which doesn’t have a chiral center around which its mirror image can “flip”. Molecules that have the
same molecular formula, but
However, most D-amino acids can be converted to L- amino acids (via different arrangements of
enzymes called D-amino acid oxidases and transaminases). Exceptions are the atoms.
D-arginine, D-cystine, D-histidine, D-lysine, and D-threonine.
Mirror
CHIRAL CENTER
The chemical “middle” of
NH2 NH2 a mirror-image molecule;
an atom that’s bonded
to four different chemical
components
H C R R C H
ENZYMES
Proteins that facilitate
chemical reactions (e.g.,
breaking down molecules)
COOH COOH
FIGURE 9
L-Amino acid D-Amino acid L and D amino acids

Amino acid metabolism DEAMINATION

The removal of an amino
Unlike fats and carbohydrates, we don’t use proteins much for fuel; rather, our group from an amino acid
bodies tend to save them for other jobs, such as tissue rebuilding. molecule
Amino acids are also metabolized differently than fats and carbohydrates. In UREA CYCLE
order to use their carbons and hydrogens, the amino, or nitrogen-containing, Aka ornithine cycle, the
group needs to be removed. This process is called deamination. conversion of ammonium
ions during protein
Deamination is simple enough with the right enzyme, but it produces metabolism, which
ammonium ions (NH4+), which are toxic. Our bodies have another process, produces urea
called the ornithine or urea cycle, to remove ammonia by converting it into
KREBS CYCLE
urea ((NH2)2CO). We then excrete the urea in our urine. (Fun fact: Hans Krebs,
A biochemical process
who discovered the Krebs cycle of energy transfer in the body, also discovered as a part of energy transfer.
the urea cycle.)
GLUCOGENIC
While all amino acids can be used for energy, our bodies can convert certain
Glucose-producing
glucogenic amino acids into glucose. Others, known as ketogenic amino acids,
can be converted into ketone bodies. Many can be converted to either. KETOGENIC
Ketone-forming
Gluconeogenesis
When our bodies convert glucogenic amino acids into glucose, the simple GLUCONEOGENESIS
sugar that’s the main basis for making ATP, or our body’s energy currency, The process of creating
the process is known as gluconeogenesis (gluco = glucose, neo = new; glucose from non-
carbohydrate sources
genesis = creating).
Glucogenic and ketogenic amino acids in humans
GLUCOGENIC GLUCOGENIC AND KETOGENIC KETOGENIC
Arginine Isoleucine Leucine

Asparagine Phenylalanine Lysine
Aspartic acid Tryptophan
Cysteine Tyrosine
Glutamic acid
Glycine
Histidine
Serine
Valine
Methionine

Peptides KETONE BODIES

Compounds (primarily
acetoacetate,
A peptide is made of two or more amino acids bonded together. ß-hydroxbutyrate and
acetone) made in the
Proteins and peptides are organized into complex, distinctive three-dimensional
liver from fatty acids
structures. (and sometimes protein)
when there is not enough
But amino acids don’t make peptides randomly. Rather, they have a specific
carbohydrate for energy.
order, much like spelling out words. Letters together in a specific order give you
a word; amino acids in a specific order give you a specific protein. This is called
primary structure. If you know the sequence of a given protein’s gene, you can
guess its primary structure.
Naming convention for peptides
NUMBER OF NUMBER OF
AMINO ACIDS NAME AMINO ACIDS NAME
1 amino acid 7 heptapeptide
2 dipeptide 8 octapeptide
3 tripeptide 9 nonapeptide
4 tetrapeptide 10 decapeptide
5 pentapeptide 2 to around 202 oligopeptide
6 hexapeptide 25 to thousands polypeptide (protein)
2 There’s no hard cut-off here.
Depending on how the order of amino acids, different parts of proteins can fold GLUCOSE
A simple sugar
into a helix or into sheets as their secondary structure.
• Helixes look similar to what a pipe cleaner would look like if you wrapped ATP
part of it around a tube. Our body’s energy currency.
Abreviations of adenosine
• Sheets look the rest of the pipe cleaner folding back on itself over and over
triphosphate.
again to make a sheet-like structure.
A protein can have both helixes and sheets throughout its structure. PRIMARY STRUCTURE
The sequence of amino
The next level of structure, tertiary structure, is how the different folds of the acids in a peptide

proteins fit together to make a three-dimensional configuration. Taking our pipe SECONDARY STRUCTURE
cleaner from above with a helix and sheet, it would fold a different way so Formation of protein helixes
or sheets from peptides
that the helix and sheet fit together. This is because certain amino acids (like
cysteine) tend to make bonds with other amino acids.
Protein structures
Level LEVEL Description

DESCRIPTION Stabilized byBY
STABILIZED
Level
Level Description
Description Stabilized
Stabilized byby
Level Description Stabilized by
Primary The sequence of amino acids Peptide bonds
Primary
Primary The The sequence
sequence of amino
of amino acids Peptide bonds
Primary The sequence
in a apolypeptide ofacids
amino acids Peptide bonds
Peptide bonds
Primary The sequence
in ainpolypeptide
polypeptide
in a polypeptide
of amino Peptide bonds Gly Ser Asp Cys
Gly
Gly Ser Asp Cys
Gly Ser Ser Asp Asp Cys Cys
acids in a polypeptide
Secondary Formation ofofα-helices

Formation and β-pleated Hydrogen bonding between groups
Secondary
Secondary
Secondary Formation
Secondary Formation
sheets ininof of of
α-helices
α-helices
Formation ɑ-helices
and
and β-pleated
β-pleated
α-helices
aapolypeptide
Hydrogen
and β-pleated Hydrogen
Hydrogen
along the
bonding
bonding
bonding
Hydrogen between
between
between
bonding
peptide-bonded
groups
groups
between groups
backbone
sheets
sheets and polypeptide along the peptide-bonded backbone
insheets ß-pleated
a polypeptide sheets in groups
in a polypeptide along
along the the the peptide-
peptide-bonded
along backbone
peptide-bonded backbone
a polypeptide bonded backbone

α-helix
α-helix sheet
β-pleatedsheet
β-pleated
α-helix
α-helix sheetsheet
β-pleated
β-pleated
Tertiary Overall
Tertiary
Tertiary
Tertiary Tertiary Overall
Overall
Overall three- shape
three-dimensional
three-dimensional
Overall
three-dimensional
shape
shapeshape
three-dimensional Bonds
Bonds
Bonds
Bonds
andandother
and
Bonds other interactions
interactions
otherother
and
andR-group,
other
interactions
interactions
interactions
ofofa apolypeptide
polypeptide between
between R-group, or between
dimensional shape of a
of a polypeptide
of a polypeptide between
between
R-groups
R-group,
between
and
R-group,
R-group,theor or orbetween
between
between
R-groups the peptide-bonded
and and
R-groups the peptide-bonded
polypeptide R-groups
R-groups
backbone and the peptide-bonded
and the peptide-
backbone
backbone
backbone
bonded backbone
Quaternary
Quaternary Shape
Quaternary
Quaternary ShapeShape
Shape
producedproduced
produced
producedby by combinations
bycombinations
combinations Bonds
Bonds
Bondsand
andother
Bonds
and and
other interactions
otherother interactions
interactions
interactions
Quaternary Shape produced
ofofpolypeptides.by combinations
of polypeptides.
polypeptides. Bonds andR-groups,
other
between
between
between interactions
R-groups,
R-groups, and and between
between
by combinations
of polypeptides. of between
between R-groups,
R-groups,
peptide
peptide
peptide backbones
backbones and
backbones and
between
of different
of different
polypeptides peptide
between backbones
peptide ofbackbones
polypeptides
polypeptides
polypeptides different
polypeptides
of different polypeptides
The last level of structure, quaternary structure, involves more than one TERTIARY STRUCTURE
peptide together. We can take our first pipe cleaner structure and bind it to a Three-dimensional shape
of a structure built from
second pipe cleaner structure (and, theoretically, as many other pipe cleaner
complex peptides (i.e.
structures as we like), and create an even bigger, more complex configuration. polypeptides)
Conjugate proteins: Glycoproteins and lipoproteins

QUATERNARY STRUCTURE
Conjugate proteins are proteins with nonprotein parts. A few of the more Arrangement of many
common conjugate protein types are glycoproteins (carbohydrates + subunits within a large
protein), lipoproteins (fat or cholesterol + protein) and phosphoproteins protein
(phosphate+protein).

Most conjugate proteins are glycoproteins. They’re usually found on the outside CONJUGATE PROTEINS
of the cell membrane or part of the immune system (as immunoglobulins such Proteins with non-protein
parts
as IgA, IgG, IgE and so on).
Examples of conjugate proteins include:
GLYCOPROTEINS
• C-reactive protein (CRP) is a well known glycoprotein associated with low- A carbohydrate-protein
level inflammation and insulin resistance. complex
• Thyroid stimulating hormone (TSH), follicle stimulating hormone (FSH) and

LIPOPROTEINS
luteinizing hormone (LH) are hormones that are glycoproteins.
A lipid-protein complex
• Low-density lipoprotein (LDL) and high-density lipoprotein (HDL) are the
most well-known lipoproteins that allow lipids to move around in a body
PHOSPHOPROTEINS
that’s mostly water.
A phosphate-protein
complex
Collagen
Collagen is found in connective tissue like tendons, cartilage, the non-mineral
IMMUNOGLOBULINS
component of bone, and pretty much anywhere you need cells to stick together. Antibody proteins in the
Collagen is made up mostly of a repeating primary amino acid sequence of immune system
glycine-proline-4-hydroxyproline. This creates a special type of tightly twisted

and packed helix structure, which makes collagen very strong. In fact, collagen
C-REACTIVE PROTEIN
has more tensile strength than steel wire of comparable size.
A glycoprotein associated
Collagen made by vertebrates is about 35% glycine, 21% proline and with low-level chronic
hydroxyproline, and 11% alanine. (The other 33% includes other amino acids inflammation and insulin
resistance
that vary from species to species.) Hydroxyproline is an uncommon amino
acid and not listed in the 20 amino acids, because it’s made as a byproduct
after proline is produced. If you don’t have enough vitamin C, less proline will
LOW-DENSITY
convert to hydroxyproline.
LIPOPROTEIN (LDL)
Collagen has little nutritional value, as it’s extremely low in essential amino One of five major lipoprotein
acids. However, some preliminary research, based on measuring levels of groups that transport
triglycerides, fatty acids,
procollagen I (a collagen precursor) in blood, suggests that taking 15 grams of
phospholipids, and
gelatin + 48 mg of vitamin C one hour before exercise may stimulate collagen cholesterol to the body;
synthesis in tendons and ligaments. sometimes refered to as
“bad cholesterol”
Fun fact: Gelatin (Jello) is nearly identical to collagen. It’s derived from
collagen, and has the same amino acid structure: Both are particularly high
in glycine, proline, and hydroxyproline. The difference between gelatin
and hydrolyzed collagen, though, is that collagen can’t form a gel. There
doesn’t seem to be any difference between gelatin and collagen in whether
procollagen I is produced.

Proteins as players in chemical processes HIGH-DENSITY

LIPOPROTEIN (HDL)
Amino acids, peptides, and proteins are involved in many reactions in the One of five major lipoprotein
body beyond making new structural proteins. For example, proteins known as groups that transports
cholesterol to the liver as a
enzymes can help chemical reactions happen.
part of reverse cholesterol
Two more important processes for amino acids are the production of creatine transport; sometimes
and choline. referred to as “good
cholesterol”
Through a series of reactions, the amino acids glycine and arginine produce
creatine, which is used for short term energy storage as phosphocreatine (PCr).
Creatine can be further metabolized in active muscle to produce creatinine, CREATINE
which can be used to estimate muscle mass. (However, since creatinine is An amino acid that
also used to detect kidney dysfunction, serum creatinine can be a false positive is a component of
phosphocreatine, a
for kidney dysfunction in people who have more muscle. Cystatin C may be a
compound needed to quickly
better test for people with higher muscle mass.) make more ATP under
intense energy demand
Choline is made from serine and is essential for neurotransmitters (such as
acetylcholine), cell membrane components (phosphocholine), the myelin
sheath, and even epigenetic modifications. CHOLINE
An essential nutrient
Protein digestion and absorption involved in synthesizing and

transporting lipids, as well as
methyl group metabolism
The stomach
Protein digestion really gets started in the acidic environment of the stomach.
Hydrochloric acid (HCl with a concentration of 160 mM) and the enzyme pepsin
(the active form of pepsinogen) begin to break down proteins. Then, the resulting
peptides and single amino acids are passed along to the small intestine.

Protein denaturation These structural changes change the

behavior of the protein, such as whether it
Part of the digestion process is the can dissolve in water, or how it reacts with
denaturation of proteins. other proteins. For instance, denatured
Denaturation is the change in the three- hemoglobin can’t bind oxygen, while
dimensional structure of the protein. denatured creatine kinase can’t attach a
Scientists sometimes call this “unfolding” of phosphate to creatine. A denatured protein
the protein, because key bonds that keep is fundamentally different than one with its
it folded are broken (usually hydrogen and higher structure.
sulfide bonds). While it seems like denaturation might be a
Denaturation can be caused by factors bad thing, it’s not necessarily.
such as heat (i.e., cooking), alcohol, strong For example, denaturing proteins during
bases, or exposure to stomach acid. cooking helps us absorb them better. Then,
Different proteins denature at different denaturation during digestion helps proteases
temperatures and pH levels. The enzyme (enzymes that break down proteins) access
pepsin that’s found in the stomach does not those proteins more effectively.
denature there; in fact it does its work best
in the stomach’s highly acidic pH of 2.
The small intestine DENATURATION

A change in the three-
Once in the small intestine, enzymes from the pancreas (such as trypsin, dimensional structure of the
chymotrypsin, carboxypeptidases, aminopeptidases, and collagenase) further protein
break down proteins. Peptides must be short — fewer than 4 amino acids
long — to be absorbed. The cells that line the small intestine (enterocytes) PROTEASES
break down peptides even further, so that nearly all former proteins enter the Enzymes that break down
bloodstream as single amino acids. proteins
For example, when you eat collagen, it’s digested and absorbed into the body
as peptides or as single amino acids, not as a whole protein. The parts of
ENTEROCYTES
collagen enter your bloodstream, but not the full collagen protein.
Intestinal cells

The liver
Most amino acids go to the liver via the portal vein. For every 100 g of amino
acids taken in, about 80 g will go to the liver.
Of that:
• About 20 g will be used for protein synthesis in the liver.
• About 60 g will be broken down, or catabolized, in the liver.
• About 20 g will be exported by the liver into systemic circulation.
For every 100 g

Liver 80 g
of amino acids
ingested:
Catabolized 60 g
Protein synthesis 20 g
Remains in liver 14 g
Exported to plasma 6 g
Systemic circulation 20 g
Protein synthesized in the liver FIGURE 10

On average, how 100 g of
Of the 20 g of protein synthesized in the liver: ingested amino acids are
distributed in the body
• 14 g will remain in the liver
• 6 g will be exported to the plasma in the form of plasma proteins (albumin,
globulins, lipoproteins, etc.), glutathione, carnitine, creatine, and other
compounds.
Within the liver, proteins can be turned into enzymes and nitrogen-containing
chemicals for the liver to use.

Proteins broken down in the liver

The liver will remove the amino group (NH2) from about 60 g of protein to
produce energy, glucose, ketone bodies, or fatty acids. Exactly what happens
here will depend on factors like:
• which amino acid is being broken down (e.g., some amino acids can only
be used to make glucose);
• what other nutrients are available;
• how much energy is available (i.e., are we fasted or fed?); and
• what our body needs.
Proteins exported from the liver

Whatever the liver doesn’t use, it sends out to the plasma amino acid pool PLASMA AMINO
ACID POOL
(i.e., our body’s stores of amino acids) and other cells of the body. Our body’s
The body’s stores of
cells can then extract amino acids from the plasma for various tasks, such as
available amino acids
synthesizing: circulating in blood
• muscle proteins
• skeletal and connective tissues (e.g., bones, tendons, ligaments, cartilage)
• neurotransmitters
• enzymes
• immune system chemicals (e.g., immunoglobulins, antibodies, cytokines)
• transport proteins (e.g., carrier proteins, lipoproteins)
Amino acids
Amino group Carbon skeleton

(ɑ-keto acid)
Ammonia Urea Fatty acids Energy

FIGURE 11
Ketone bodies Glucose Where amino acids can go
after they are catabolized
Excreted into the Excreted by
intestinal tract the kidneys

Where new proteins end up depends on:

• genetic signalling;
• which amino acids are involved; and
• how much energy is available in the body.
Why is dietary protein important?

As we’ve seen, we need proteins for our body to work. Proteins are crucial for
nearly every aspect of cell function (as enzymes, transporters, and hormones)
and they are the major structural component of all cells in the body.
Because protein turnover is always occurring; because there are several
essential and conditionally essential amino acids that we can’t make ourselves;
and because we lose some amino acids in various metabolic processes, we
need to keep replenishing the supply. Protein deficiency can lead to anemia,
physical weakness, edema (water retention and swelling), vascular dysfunction,
and impaired immunity.
How much protein do you need?

The million-dollar question: How much protein should you eat?
The answer: It depends.
Adequate protein intake

The average person eating a standard Western diet is probably not protein
deficient. This is because most of these eaters are relatively sedentary
omnivores, which means:
• They don’t need much protein for repair or rebuilding.
• They probably eat animal products and dairy, both of which are common
sources of protein.
Yet “not grossly deficient” or “enough protein so you don’t die” doesn’t mean
optimal.
There are different standards of “adequate”, depending on ways of
measurement and the criteria used (e.g. preventing malnutrition versus
enhancing performance and recovery). As the table below shows,
recommendations can vary significantly.
Newer recommendations based on more updated methods (such as the IAAO)
suggest that higher protein is better.

Daily protein recommendations for adults by body weight
SUGGESTED DAILY PROTEIN INTAKE
GRAMS PER KILOGRAM GRAMS PER POUND
Estimated Average 0.66 0.3

Requirement (EAR)
Recommended Dietary 0.8 0.36

Allowance (RDA)
Acceptable Macronutrient 1.05-3.67 0.48-1.66

Distribution Range (AMDR)
(Also expressed as 10-35%
of total caloric intake a day)
Indicator of Amino Acid 1.0-1.2 for adults 0.45-0.54 for adults

Oxidation (IAAO) method 1.2-1.4 for 65+ 0.54-0.64 for 65+
(2008)
American College of Sports 1.2-2.0 0.54-0.9

Medicine Joint Position
Statement: Nutrition and
Athletic Performance (2016)
Optimal protein intake

Recent evidence strongly suggests that we need more protein than previously
recommended if our goal is to look, feel, function, perform, recover, and age
better. (So, pretty much most goals.)
Our protein needs can go up if:
• we’re training hard frequently (e.g., as athletes) or have a heavy physical job;
• we want to gain lean mass and/or strength;
• we’re injured or sick, or are recovering from surgery;
• we’re older (because we digest protein less well, so we need more to meet
requirements); and/or

• we’re losing protein for some other reason (e.g., chronic physical stress).
We may need more protein if we’re trying to lose weight, which can put us in a
negative energy balance. Protein helps keep us feeling full longer.
While most people will do best with slightly more protein, some may have
health conditions that require a lower-protein diet.
PHENYLKETONURIA (PKU)
These can include: An inherited metabolic
disease that causes a
• kidney disease build-up of the amino acid
• certain metabolic diseases (e.g., PKU) phenylalanine
• liver disease
• problems with gastric emptying
HOMOCYSTINURIA
• homocystinuria An inherited metabolic
disease that causes a
Unless there’s a specific medical reason for a low protein intake, most buildup of homocysteine and
people will benefit from eating relatively more protein. its metabolites
Low
<0.8
Prevent malnutrition
Adequate
0.8 - 1.2*
Sedentary
Adequate
1.2 - 1.6
Active but overweight/obese
Adequate
Active with healthy weight or 1.6 - 2.2
body composition
High
Healthy and looking to change 1.6 - 3.3
weight/body composition
0 0.5 1.0 1.5 2.0 2.5 3.0 3.5
Grams of protein per kilogram of bodyweight per day
* Growing evidence suggests 1.2 g / kg might be a more appropriate minimum, particularly for older adults
Currently, recommendations for optimal protein intake range for building and FIGURE 12
maintaining muscle range from 1.6-2.2 g/kg (0.73-1.0 g/lb) per day, though General recommendations
some suggest that people losing body fat while maintaining lean mass should for daily protein intake
based on body composition
shoot for 2.3-3.3 g/kg (1.04-1.5 g/lb) per day.
and goals
There are no current recommendations for optimal protein intake for pregnant
or breastfeeding women.

Essential amino acid intake

Beyond total protein intake, it’s also important to get essential amino acids from
our diet consistently — we can’t just “top off” these indispensable amino acids
one day and be fine for the rest of the week.
Recommended intakes of essential amino acids for adults
ESTIMATED AVERAGE RECOMMENDED DAILY

AMINO ACID REQUIREMENT (EAR) ALLOWANCE (RDA)
MILLIGRAMS/KILOGRAM/DAY
Leucine 34 42
Isoleucine 15 19
Valine 19 24
Lysine 31 38
Threonine 16 20
Tryptophan 4 5
Methionine + cysteine 15 19
Phenylalanine + tyrosine 27* 33
Histidine 11 14
*Has a much wider range compared to other amino acids — 15.1 to 39.
However, there’s no need to supplement specific EAAs if you’re choosing

all kinds of different high-protein foods consistently. (We’ll look more at
implementation in Unit 3.)

Carbohydrates
What are carbohydrates?
Carbohydrates are macronutrients made up of long chains of smaller units SACCHARIDES
called saccharides, or sugars (from the Latin saccharum, or sugar). Sugar molecules
Simple carbohydrate molecules (aka simple sugars) have a basic ring structure
of carbons and hydrogens. MONOSACCHARIDE
A single, simple sugar
• One ring is called a monosaccharide (mono = one).
• Two rings joined is a disaccharide (di = two). DISACCHARIDE
• A few rings joined are called oligosaccharides (oligo = few). Two simple sugars joined
together
As carbohydrates link together in more intricate structures (hence the term
“complex carbohydrates”), they become glycogen, starches, and various types of
OLIGOSACCHARIDES
soluble and insoluble fibers. We often call these polysaccharides (poly = many).
A few simple sugars joined
together
GLYCOGEN
The storage form of a
complex starch in muscle
and liver tissue
Monosaccharides Disaccharides Amylose Amylopectin POLYSACCHARIDES

(e.g., glucose) (e.g., sucrose) Complex carbohydrates
Simple sugars Starches
Unlike proteins, carbohydrates don’t contain nitrogen, which allows them to be FIGURE 13
metabolized more easily in processes that transfer energy within our bodies. Sample carbohydrate
structures
The chemical description of carbohydrates is Cn(H2O)n or, in English, one
carbon for one water, giving carbohydrates their name (carbon + hydrate,
aka water). The ratio of water to carbon has to be 1:1 for a molecule to be a
carbohydrate. Carbohydrates’ water-binding effect means that we’ll store about

3-4 grams of water per gram of stored carbohydrate in our bodies, and that
if we cut out carbohydrates, we’ll quickly lose body water (which leads to the
dramatic initial weight loss on a low-carbohydrate diet).
Three major classes of carbohydrates
MONOSACCHARIDES DISACCHRIDES POLYSACCHARIDES
Glucose Sucrose Digestible

Fructose Maltose Starch and dextrins
Galactose Lactose Glycogen
Mannose Trehalose Partially digestible
Ribose Inulin
Raffinose
Indigestible
Cellulose
Pectin
Saccharides
Monosaccharides, simple single sugars, are the units that make up
carbohydrates.
Categorizing monosaccharides
Like the amino acids that build proteins, it may be helpful to imagine
monosaccharides as Legos that can fit together in different ways to make
different carbohydrates. However, unlike amino acids, the stereoisomer
version of monosaccharides that we use is the dexter or D version (you might
remember that the amino acids our body uses are L-amino acids).
Our bodies can’t metabolize L-monosaccharides.
Monosaccharides follow this chemical ratio (CH2O)n, with n having to be equal
to or more than 3, and range from 3 to 9 carbons in size. For example, both
glucose and fructose, key monosaccharides in human metabolism, share the
formula C6H12O6.
Unlike amino acids, which must be used as specific building blocks for
proteins (as dictated by DNA), monosaccharides can, in most cases, be used

or processed interchangeably. However, they can still be classified and used

differently based on their biochemical and physical configuration.
More complex saccharides, made up of monosaccharides bonded together, are
grouped by how many monosaccharides they have.
Classification of saccharides by number of monosaccharide units
NUMBER OF NUMBER OF
MONOSACCHARIDE MONOSACCHARIDE
UNITS NAME UNITS NAME
1 monosaccharides 7 heptasaccharide
2 disaccharide 8 octasaccharide
3 trisaccharide 9 nonasaccharide
4 tetrasaccharide 10 decasaccharide
5 pentasaccharide 2 or more oligosaccharide
6 hexasaccharide 30 to thousands polysaccharides (carbohydrates)
Common oligosaccharides
COMMON DISACCHARIDE COMPOSITION
mannose 2 glucose units
lactose 1 glucose unit + 1 galactose unit
sucrose 1 glucose unit + 1 fructose unit*
isomaltulose (found in honey) 1 glucose unit + 1 fructose unit*
* Note: The bonds between glucose and fructose are slightly different in sucrose than in isomaltulose, though the two are isomers,
or related forms, of each other.

Polysaccharides STARCH
Storage form of carbohydrate
Polysaccharides are used for: in plants
• energy storage (such as starch in plant cells or glycogen in animal cells); GLYCOGEN
• structure (such as cellulose in plants, or chitin that helps make up the Storage form of carbohydrate
in animals
exoskeletons of insects and crustaceans such as shrimp or lobster); and/or
• mucus/joining fluid (mucopolysaccharides/ glycosaminoglycans), CELLULOSE
A type of fiber that gives
chondroitin, lubricin, hyaluronate (hyaluronic acid), heparin, dermatan,
cells a rigid cell wall
and keratin found in connective tissue, skin, synovial fluid and eyes.
Glucosamine, which you may recognize as a supplement for joint health, is CHITIN
a building block of glycosaminoglycans. A polysaccharide that helps
make up the exoskeletons of
We’ll look more at glycogen when we look at carbohydrate digestion and insects and crustaceans
absorption.
Sample polysaccharide structures
STARCH
CELLULOSE AMYLOSE AMYLOPECTIN GLYCOGEN
Source Plant Plant Plant Animal
Yes Yes
Branches No No
(~per 20 subunits) (~per 10 subunits)
Shape
Fiber MUCOPOLYSACCHARIDES/
GLYCOSAMINOGLYCANS
Plant cells have a wall that animal cells don’t. This gives plants their structure
Polysaccharides are found
and rigidity. The cell wall is mostly cellulose (a structural plant fiber), pectin in mucus, and fluids
(more fiber), hemicellulose (yet more fiber), and a little protein. Cellulose is surrounding the joints
also made up of glucose units, but it has a long, straight structure with no
coiling or branching.

Starch GLUCOSAMINE
A building block of
Plants produce glucose via photosynthesis, using the sun’s energy, and store glycosaminoglycans/
excess glucose as starch. The starch is contained within the plant’s cells, mucopolysaccharides.
organized into ball-like granules that can range from 1 to 110 μm across.
There are two forms of starch, amylose and amylopectin, which differ FIBER
significantly in their three-dimensional structures. A type of carbohydrate that
can’t be digested, and which
• Amylose is a single helical coil — think of it as a spring. gives plants their structure
• Amylopectin has helical coils that branch off from each other, with about
20 glucose per branch. This increased branching for amylopectin means it’s
easier for enzymes to get to it and break it down quickly. PECTIN
A type of soluble
Different amylose and amylopectin arrangements can affect the shape of the carbohydrate that becomes
starch granules within a cell. If you cut a granule in half crosswise, you’ll gelatinous (hence used in
see growth rings that are much like that of a tree trunk. These rings seem to jams)
correspond to plants’ dark and light cycles: Plants deposit new starch (either
amylose or amylopectin) during light cycles when photosynthesis is occurring, HEMICELLULOSE
with breaks during dark cycles. The pattern emerges as the regions alternate A type of fiber that gives
between amylose (which forms a crystal structure) and amylopectin (non- cells a rigid cell wall;
similar to cellulose but
crystalline parts).
with a different chemical
Starch digestion and absorption composition
Just like protein, carbohydrates have a 3D structure, which also affects how we
digest and absorb them. How much or how well we digest and absorb various
carbohydrates depends on:
• Chemical makeup: Which types of monosaccharides, how they’re linked,
the molecule size, etc.
• Starch source: For instance, beans, grains, starchy vegetables, etc.
• Food processing: Is the starchy food raw or cooked? Which cooking
method? Etc. For instance, we can’t digest the starch in many foods (such
as potatoes) when they’re raw. However, cooking (especially in moist heat)
causes the plant cells to swell, explode, and become viscous, which makes
the starch more digestible.
• Meal factors: What other nutrients are in the meal, such as protein, fat, and
other carbohydrates, etc.
• Biological variation: For instance, the species or age of the plant source, etc.

• Gastrointestinal handling: How much and how quickly our bodies digests
and absorbs the starch, with the small intestine handling glycemic (glucose-
yielding) carbohydrates, and the large intestine handling non-glycemic
carbohydrates such as fiber.
The AMY1 gene, Since then, things have gotten murkier. Some
studies (such as Rukh et al 2017) replicated
carbohydrate tolerance, the original findings, while others (such as
and body weight Shwan & Armour 2019) didn’t support the
original study.
Ever wonder why some people can eat
Carbohydrate tolerance is more complicated
bushels of bananas without gaining a pound,
than a single gene. For instance, there are
but you seem to gain weight by just looking
other genes for different amylases (AMY2),
at a potato?
and other factors that affect salivary amylase
Maybe it’s your genes. activity.
AMY1 is the gene that makes salivary However, it’s an intriguing part of the puzzle.
amylase. You can have more or fewer copies
For more reading, see:
of AMY1 (ranging from 4 to more than 9
copies), which means you’d make more or Carbohydrate Tolerance: Is Your Ability to Eat
less amylase. Carbs Determined By Your Genes?
In 2014 a study came out in the journal Genetics: The Universe Within
Nature (Falchi 2014) showing that people See our References list for full citations.
with fewer copies of AMY1 are more likely to
be obese.
Based on digestibility, we can sort starch into three groups. Most starchy foods
have a mix of the three in different proportions.

Starch types by digestibility
STARCH TYPE PROPERTIES & CHARACTERISTICS
Rapidly digesting starch Easily and quickly digested; because of this, tends to raise
blood glucose quickly, and tends to have a higher glycemic
index (GI) (see below)
Slow digesting starch Relatively slowly and painstakingly digested; tends not to raise
blood glucose quickly; and thus tends to have a lower glycemic
index (GI) (see below)
Resistant starch Difficult or impossible for humans to digest; though it can feed
our gut bacteria
Resistant starch during real-life digestion, and one reason

why minimally-processed whole foods
Resistant starch (RS) has been getting tend to help us lose weight.)
attention recently for its role in weight loss
• RS2 has a particular type of structural
along with metabolic and gut health.
configuration, which also makes it more
There are several types of RS: difficult for digestive enzymes to access
• RS1 is a starch that is physically and break down the starch. Two common
protected from digestion by being part examples are green bananas and raw
of a cell wall, such as in whole grains, potatoes. When ripened or cooked,
legumes, or seeds. Enzymes that break respectively, this starch becomes much
down the foods can’t penetrate the less resistant.
surface of the cell, which means that • RS3, or retrograded starch, occurs when
only a fraction of the food’s energy and starchy foods containing amylose are
nutrients can be accessed and absorbed. cooked and then cooled, which changes
(This is why whole nuts tend to yield their structural matrix to make them
only about 70-80% of their total energy more like RS2. (You’ll notice this if you

cook oatmeal and then leave it in the comparable volume (in other words, you
fridge — it becomes somewhat gelatinous can eat the same amount of food, but get
and rubbery.) less energy from foods high in RS);
• RS4 are starches that have been • RS’s ability to absorb water and swell
chemically modified during food up, adding bulk and volume in our
processing. gastrointestinal tract, which in turn helps
us feel full;
• RS5 are starches that are part of a larger
complex bonded to fats (like RS4, often • offering food for our gut bacteria, which
created during food processing), which can help keep our gut microbiome
also makes it more difficult for enzymes healthy and increase the production of
to break down the starch other beneficial substances (such as
short-chain fatty acids); and
RS isn’t a magical health or weight loss
solution, although it’s a great thing to • the fact that foods naturally rich in RS
include in your diet. The benefits of resistant are minimally-processed whole foods that
starch probably come from: are relatively lower in calories, higher in
water, and contain a plethora of vitamins,
• less energy being absorbed overall,
minerals, and phytonutrients that
compared to more bioavailable starch of
promote overall health and well-being.
Carbohydrate digestion and absorption GLYCEMIC INDEX (GI)

A measure of how quickly
a carbohydrate containing
Carbohydrate digestion and absorption occurs throughout the GI tract, and food increases blood glucose
begins the moment we put carbohydrate in our mouth. post-meal
The mouth
As soon as we take a bite of carbohydrate, salivary amylases (enzymes that RESISTANT STARCH
break down starch) help to hydrolyze, or break down, saccharides into smaller A type of starch with a
carbohydrate chains. molecular configuration that
makes it difficult to digest
Salivary amylase, however, can only help with about 20% of carbohydrate
breakdown, depending on how long food stays in our mouth. The less we chew,
the faster we swallow, and the less salivary amylase has a chance to work on our
food. Conversely, if we eat slowly and chew well, we digest our food better with
the help of these salivary enzymes. (A good reason to eat mindfully.)

The stomach RETROGRADED STARCH

Resistant starch created
After the carbohydrate-containing food is swallowed, it travels down the by cooking starchy foods
esophagus to the stomach. in moist heat, then cooling
them
In the stomach, carbohydrates (and all other swallowed food) get mixed into a
homogenous mixture known as chyme. No further digestion of carbohydrates
happens here, as stomach acid designed to destroy potentially harmful
pathogens temporarily stops the action of salivary amylase.
SHORT-CHAIN FATTY
ACIDS
The small intestine
Special types of fatty acids
Once the carbohydrate is passed on to the small intestine, pancreatic amylases that are shorter than 6
take over, turning these smaller carbohydrate chains into disaccharides. carbons long, made by our
gut bacteria
• The enzyme maltase breaks down maltose into two monosaccharide units
of glucose.
• The enzyme lactase breaks down lactose (milk sugar) into glucose and
galactose monosaccharides. If you lack this enzyme, the lactose in dairy will
cause indigestion.
• The enzyme sucrase breaks down sucrose (table sugar) into glucose and
fructose monosaccharides.
Remember, starch is made up exclusively of glucose molecules joined together
into long chains. Thus, the end products of starch digestion are always glucose
monosaccharides.
All of these monosaccharide end products pass through the intestinal cells into
blood vessels that take them to the liver (via the portal vein) before they enter
general circulation.
The liver
The liver takes what it needs for energy transfer and glycogen storage and then
ships the rest out as glucose monosaccharides.
You may have noticed that we can absorb galactose and fructose from our diet,
but they don’t usually end up in the bloodstream. Why not?
• First, they’re both mostly converted to glucose by the liver. If there’s any
leftover glucose that the liver doesn’t think we need, it’ll turn that into
triglycerides (especially in times of caloric excess).
• Second, our liver actually prefers to use fructose rather than glucose for
energy and liver glycogen replenishment (though it can use glucose too).

Again, once the liver takes what it needs and does the appropriate chemical
alchemy, the glucose units released into circulation work their way through
the blood until they’re taken up into our cells.
The bloodstream and glucose

On average, we move about 20 g of glucose through our blood every hour. Our
body prefers to keep this more or less stable.
If our blood sugar drops too low, the body will immediately use the new glucose
supply for preserving blood glucose levels and for immediate energy.
If our blood sugar goes too high, the liver and muscles will take up what they
can. The liver can store about 80-100 g of glycogen before it’s full. And the
muscles can store between 300-600 g of glycogen before they’re full (this
obviously depends on the amount of muscle mass someone has, as well as
how active they are).
If blood sugar is still too high after liver and muscle storage, extra glucose can
be converted into body fat, though that’s not as common. Instead the body
oxidizes more glucose (because there’s more available) and less dietary fat,
leading to more of our dietary fat being stored as body fat.
The glycemic index (GI)

Many of you are probably familiar with the glycemic index (GI), a measure of
how quickly and significantly a given food can raise our blood sugar.
The GI tells us how much blood sugar goes up when we consume 50 g of
usable carbohydrate from a particular food. It’s a relative measure, determined
against a specific reference food — 50 g of carbohydrate from pure glucose
— which is given a GI value of 100. Each food’s GI score is then calculated
relative to this value of 100.
In general, the less processed and higher-fiber a food is, the more complex its
carbohydrate molecules usually are. Because of this, those foods will usually
take longer to digest and have a lower GI.

Blood glucose (mmol/L)
High GI
Low GI
0 50 100 150
Time after intake (minutes)
For instance, high glycemic foods include sugar, candy, breakfast cereal and FIGURE 14
bagels. Lower glycemic foods include legumes, whole grains, and vegetables. Glycemic index (GI)
When blood glucose goes up quickly, insulin usually responds quickly. The
amount of insulin released usually matches the amount of glucose present.
This has led some people to suggest that a low-GI diet is a healthy one.
While an interesting measure of the physiological response to carbohydrate in
the diet, the GI doesn’t tell the whole story.
First, we don’t eat most foods by themselves. (When was the last time you ate
a plain slice of bread as a meal?) Since protein, fat, and fiber all change GI,
eating food as part of a meal will change the GI.
Glycemic load (GL)

Researchers often use the glycemic load (GL) as another, more realistic
measure. The glycemic load of a food is based on the glycemic index multiplied
by the serving size of the food.
While this gives a better picture of how fast or significantly blood sugar may
go up after a meal, GL still has some of the same problems as GI. And it too
doesn’t take into account the other elements the food may have to offer (fiber,
water, phytochemicals, macronutrients, etc.).
Insulin index (II)

While GI and glycemic load are somewhat useful in determining overall glucose

load, they aren’t the best predictors of insulin response to a meal, which is the
measure most closely correlated with health.
Another index, the insulin index (II), measures the amount of insulin the body
produces in response to a particular food.
Interestingly, the II does not always match the GI. You may be surprised to
know, in fact, that high-protein and high-fat foods can stimulate greater insulin
responses than you’d expect, while some high-GI foods produce surprisingly
low insulin responses.
In addition, when people with underlying insulin resistance eat moderate and
high-GI foods, their bodies produce more insulin than a healthy person’s.
Why are carbohydrates important?

Along with making various structures and substances in the body, the main job
of carbohydrates is to provide energy, either immediately (from blood glucose)
or for later (from stored liver and muscle glycogen).
Physiological requirements for carbohydrate

Our brain, the most energy-greedy of all our organs, consumes about 20% of
our total daily resting energy expenditure, and its preferred energy source is
glucose. The daily Recommended Dietary Allowance (RDA) for carbohydrates to
meet the brain’s energy needs is about 125-130 grams (500-520 calories) per
day for adults and children.
However, carbohydrates are not an essential nutrient (or macronutrient) in
the same way that certain amino acids or fatty acids are essential. Strictly
speaking, we don’t need carbohydrates to function, and our bodies can make
them from other things, such as amino acids (via gluconeogenesis) to meet the
body’s need.
If we manufactured that 125-130 grams of glucose in the absence of
dietary carbohydrate, about 40% of that glucose would come from fat (via a
component of triglycerides known as glycerol, which we’ll look at in the section
on fat), and about 60% would come from gluconeogenic amino acids. GLUCONEOGENIC
The conversion of non-
In some situations, such as particular medical conditions, people may choose
carbohydrate precursors
low-carbohydrate and ketogenic diets. (For more on ketogenic diets, see our (such as specific amino
article: The Ketogenic Diet: Does It Live Up To The Hype?) In these cases, acids and glycerol) into
clinicians suggest that those on a very low-carbohydrate diet eat 100 to 150 glucose
grams of protein daily to meet glucose production needs and maintain a

positive nitrogen balance.

However, as with protein, adequate is not necessarily the same as optimal.

• Some people, especially most athletes, will feel, perform, and recover better
with relatively more carbohydrate in their diet. (We’ll look more at this in
Units 2 and 3.)
• In certain stress conditions, like trauma and sepsis, which require more
energy for recovery and rebuilding, carbohydrates can dramatically improve
outcomes.
• Carbohydrate-containing foods, especially minimally-processed whole foods,
also contain a vast array of other nutrients (such as vitamins, minerals, and
phytonutrients) along with water and fiber. PHYTONUTRIENTS
Plant nutrients
• When building muscle, carbohydrates help to enhance anabolic signaling
(i.e., cellular communication that encourages nutrient storage, growth, and
repair). For many people looking to add muscle and mass, carbohydrates
may be important. ANABOLIC SIGNALING
Cellular communication
As always, it depends.
that encourages nutrient
storage, growth, and repair
Fiber
• Fiber, while not digested and absorbed in our small intestine, plays an
important role in health.
• Fiber delays stomach emptying rates, and expands in the small intestine
slowing absorption. Both of these help us feel fuller, longer.
• Fiber can bind to substances such as cholesterol or hormones, helping
excrete excess from the body.
• Fiber can increase gastric motility in the small and large intestine, adding bulk,
absorbing water, and moving food through. Result: Good, regular poops!
• Fiber, along with resistant starches, are fermented by the microbiota in your
large intestine, to make short chain fatty acids (SCFA), carbon dioxide (CO2),
CH4 (methane), H (hydrogen) and heat. SCFA are then absorbed by the
large intestine, where the cells of the large intestine (colonocytes) use SCFA COLONOCYTES
for energy. Having healthy, diverse, and thriving gut bacteria is closely linked Cells of the large intestine
to our overall health and function. (colon)
Recommended fiber intake:

Adults up to age 50: 25 g for women and 38 g for men
Over the age of 50: 21 g for women and 30 g for men

Potential effect of fiber and resistant starches on physiology
LOCAL SYSTEMIC
 Fecal bulk  Cholesterol
 Bacteria  Triglyceride
 SCFA production  NH3
 Mineral absorption  Urea
 B vitamin synthesis  B vitamins  Immune function
How much carbohydrate do you need?

As always, the answer is: It depends.
In Unit 2, we’ll look at calculating carb intake based on activity, using this
rough guideline:
Carbohydrate needs based on activity type and bodyweight
CARBOHYDRATE INTAKE
Lightly active or sedentary ~0-1.5 g of carbohydrate per lb of bodyweight

(e.g., regular people) (~0-3.5 g/kg)
Athletes
Most strength athletes ~1.5-2.5 g of carbohydrate per lb of bodyweight
(e.g., powerlifters, weightlifters) (~3.5-5.5 g/kg)
Most intermittent, team-sport athletes ~2-3 g/lb (~4.5-6.5 g/kg)

(e.g., soccer, rugby, volleyball)
Most endurance athletes ~3-4 g/lb (~6.5-9 g/kg)

(e.g., marathon runners)
Ultra endurance athletes* ~4.5-5.5 g/lb (~10-12 g/kg)

(e.g., Ironman, ultramarathon)
* Note: Some ultra-endurance athletes perform equally well on high-fat, ketogenic-style intakes as opposed to high-carb, low-fat
intakes. For most other athletes, it can decrease performance.

Fats
What are fats?
Fats are organic molecules made up of carbon and hydrogen, joined together
in long groups called hydrocarbons. The length and arrangement of these HYDROCARBONS
hydrocarbon chains, and their interaction with each other, determines fat type. A particular type of carbon-
hydrogen molecule in a
Biochemically, this only includes a molecule called triglycerides (or chain structure
triacylglycerols). We are going to go briefly into lipids and the other types
important to humans.
Lipids
LIPIDS
Fats fall under a bigger biochemical group called lipids. A large class of water
insoluble molecules
Lipids include:
that includes fats, oils,
• fats and oils; cholesterol, and waxes
• waxes;
• some vitamins (fat-soluble);
• some hormones (steroid hormones); and
• compound lipids (phospholipids, glycolipids, and lipoproteins).
Lipids are categorized based on what they dissolve in, rather than what they
do. This means lipids as a group do lots of different things, and there are lots of
ways to classify them.
For instance, as part of your body fat, lipids offer energy storage, padding
for internal organs, and insulation. A completely different group of lipids
FATTY ACIDS
(phospholipids) make up most of your cell membranes. Yet another group of lipids
Chains of hydrogen and
(sterols) makes up steroid hormones, cholesterol and bile acids (aka bile salts). carbon that are the building
All these different types of lipids make it hard to group them, but the blocks
simplest and most applicable to humans is using structural and functional

classifications:
TRIGLYCERIDES
1. Fatty acids Three fatty acids joined
together by a glycerol
2. Triglycerides (also known as triacylglycerols), diglycerides, and
molecule; the main storage
monoglycerides form of fats in the body

3. Sterols (cholesterol, bile salts, and phytosterols) STEROLS

Lipids that have a steroid
4. Phospholipids nucleus (a center with 4
5. Sphingolipids separate carbon rings) and a
hydroxyl group
For our purposes, we’re going to focus on the first four groups, with a specific
focus on fatty acids and triglycerides.
CHOLESTEROL
A type of fat-based molecule
Fatty acids
found in most tissues;
The simplest unit of lipid, analogous to a carbohydrate monosaccharide or an crucial in metabolism
amino acid as a building block, is a fatty acid.
Fatty acids are made of simple hydrocarbon chains with special chemical BILE SALTS
groups at each end: A substance found in
bile (produced by the
• a methyl group (CH3) on one end (often known as the “omega” end, and gallbladder) that helps us
written as ω); and digest fats
• a carboxyl group (COOH) on the other (often known as the “alpha” end and
written as ɑ).
PHYTOSTEROLS
The carboxyl group is hydrophilic (or “water-loving”, i.e., can be dissolved in Plant-based sterol
compounds with potential
water), while the methyl group is hydrophobic (or “water-fearing”, i.e., does not
health benefits
dissolve in water). However, most fatty acids don’t dissolve in water, because
the methyl groups are repeated within the structure more often.
SPHINGOLIPIDS
A class of lipids with
particular activity in our
H H H H H H H H H H H H H H H nervous system
O
Palmitic acid H C C C C C C C C C C C C C C C C
(16 carbons)
OH PHOSPHOLIPIDS
H H H H H H H H H H H H H H H
Lipids (diglycerides) with a
Methyl Carboxyl
phosphate group attached
OMEGA ( Ω ) END ALPHA ( α ) END
Fatty acids can vary in: FIGURE 15

Sample fatty acid structure
• length (number of carbons);
• saturation of hydrogen (saturated, monounsaturated, polyunsaturated); and
• isomerization (trans or cis).
With these three variables combined, there are many different types of fatty acids.

Length SHORT-CHAIN FATTY

ACIDS (SCFA)
Fatty acids range in size from four to about 24 carbons, most commonly 16 Fatty acids with fewer than 6
and 18 carbons long. carbons
Fatty acids can be named based on length:

MEDIUM-CHAIN FATTY
• Short-chain fatty acids (SCFA): Fewer than 6 carbons long (as we saw in ACIDS (MCFA)
the section on carbohydrates, our gut bacteria can make these for us). Fatty acids between 6 to 12
carbons long
• Medium-chain fatty acids (MCFA): Between 6 and 12 carbons long.
Medium-chain triglycerides (MCTs) are a specific type of triglyceride (more
MEDIUM-CHAIN
about those below) that have two or three MCFAs as their fatty acids. TRIGLYCERIDES (MCTS)
• Long-chain fatty acids (LCFA): Between 13 to 21 carbons long. A type of triglyceride that
have two or three MCFAs as
• Very long-chain fatty acids (VLCFA): 22 or more carbons long. their fatty acids.
Each fatty acid is named based on how long it is, and the number of double
bonds it contains. LONG-CHAIN FATTY ACIDS
(LCFA)
Part of the name also counts the carbons from the omega (ω, or methyl) end, Fatty acids between 13 to
to the first double bond. So, omega-3 fatty acids have the first double bond 3 21 carbons long
carbons from the omega end, while omega-6 fatty acids have the first one at 6
carbons along. (More on this in a moment.)
VERY LONG-CHAIN FATTY
ACIDS (VLCFA)
Fatty acids that are 22 or
more carbons long
OMEGA-3 FATTY ACIDS

A group of polyunsaturated
fatty acids with a double
bond 3 carbons from
the omega / methyl end.
The essential fatty acid
α-linolenic acid (ALA) is an
omega-3 fatty acid.
OMEGA-6 FATTY ACIDS

A group of polyunsaturated
fatty acids with a double
bond 6 carbons from the
omega / methyl end. The
essential fatty acid linoleic
acid (LA) is an omega-6
fatty acid.

Fatty acid naming convention with common name and omega categorization in brackets
NUMBER OF SATURATED MONOUNSATURATED POLYUNSATURATED

CARBONS FATTY ACIDS FATTY ACIDS* FATTY ACIDS*
4 Butanoic (butyric)
6 Hexanoic (caproic)
8 Octanoic (caprylic)
10 Decanoic (capric)
12 Dodecanoic (lauric)
14 Tetradecanoic
(myristic)
16 Hexadecanoic (9Z)-9-Hexadecanoic
(palmitic) (palmitololeic; omega-7)
18 Octadecanoic (9Z)-9-Octadecenoic 9, 12 Octadecenoic (linoleic,

(stearic) (oleic, omega- 9) omega-6)
9, 12, 15 Octadecenoic
(α-Linolenic acid (ALA),
omega-3)
20 Eicosanoic (Z)-octadec-11-enoic acid (5Z,8Z,11Z,14Z)-5,8,11,14-

(arachidic) (gadoleic, omega-7) Eicosatetraenoic acid
(arachidonic acid, omega-6
fatty acid)
icosa-5,8,11,14,17-
pentaenoic acid
(eicosapentaenoic or EPA,
omega-3)
22 Docosanoic (Z)-docos-13-enoic acid (4E,7E,10E,13E,16E,19E)-

(behenic) (erucic, omega-9) docosa-4,7,10,13,16,19-
hexaenoic acid
(docosahexaenoic (DHA,
omega-3)
*this is a partial list

Saturation SATURATED FATTY ACIDS

Fatty acids with a complete
Hydrogen atoms can bond to the hydrocarbon chain. This is known as set of hydrogens bonded to
saturation. The more hydrogens bonded, the more saturated the fat is. the carbons and no double
bonds in the hydrocarbon
You can think of saturation as a bit like cars taking up spots in a parking lot. skeleton
If hydrogens have filled up all the available bonding spots on the chain (or the
cars have parked in all the spaces), the fat is saturated. If only some hydrogens
have bonded, the fat is unsaturated. Where hydrogens are missing, there is a
double bond between the carbon atoms.
Saturated fats Unsaturated fats

All hydrogens full Missing hydrogens
Unsaturated fatty acids can be broken down into: FIGURE 16

Saturated versus
• monounsaturated fatty acids (in which only one carbon is unsaturated, or unsaturated fats
missing a hydrogen); and
• polyunsaturated fatty acids (in which more than one carbon is unsaturated,
thus missing four or more hydrogens).
Note: Due to chemical structure, the shortest monounsaturated fatty acid is 14 MONOUNSATURATED
carbons long and the shortest polyunsaturated fatty acid is 16 carbons long. FATTY ACIDS
Fatty acids without a
Because unsaturated fats tend to have a double bond where they’re missing complete set of hydrogens
hydrogens, there’s a “kink” or a bend in their physical shape. They can’t pack and one double bond
together as tightly, which means they’re usually liquid at room temperature. The between two carbons
less saturated the fat, the more fluid it is.

POLYUNSATURATED FATTY
(Indeed, polyunsaturated omega-3 fatty acids act like “natural antifreeze” for ACIDS
cold water fish, preventing their cells from stiffening up in icy temperatures.) Fatty acids without a
complete set of hydrogens
Conversely, saturated fats are straight, and can pack tightly together. Given this and two or more double
chemical structure, saturated fats (such as butter, coconut oil, or cocoa butter) bonds between carbons

are usually solid or semisolid at room temperature. DOUBLE BOND

A particularly strong
Most dietary fat sources are made up of some combination of saturated, chemical bond in which two
polyunsaturated, and monounsaturated fatty acids. atoms share two pairs of
electrons
For example, while most people think eggs are high in saturated fat, eggs
actually contain more monounsaturated fatty acids than saturated fatty
acids. Indeed, 39% of the fat in eggs is saturated, while 43% comes from
monounsaturated fat and 18% from polyunsaturated fat.
39% 66% 9% 47% 22% 17%
19%
37%
31%
Fat content (%)
72%
43%
49%
47% 46%
27% Saturated fat
Monounsaturated fat
18%
Polyunsaturated fat
4% 4%
Eggs Butter Flax Beef Tofu Salmon

seeds
Isomerization: Cis- and trans-fatty acids FIGURE 17

How some foods differ
As we’ve seen, the chemical structure of saturated fats makes them straight,
in fat composition
while the chemical structure of unsaturated fats gives them at least one bend.
Like proteins and carbohydrates, fatty acids have a three-dimensional shape
that affects their function in the body.
Most naturally occurring unsaturated fatty acids have what is called a cis CIS CONFIGURATION
configuration that causes the fatty acids to bend into a U like shape around the The normal configuration
of a polyunsaturated fatty
double bond between carbons. However, some unsaturated fatty acids can take
acid; functional groups are
a trans configuration, which straightens the molecule so that it looks (and acts) on the same side of the
more like a saturated fat. hydrocarbon chain

TRANS CONFIGURATION
An unsaturated fatty acid
Cis double bond (bent)
with a particular chemical
structure that makes it
more like a saturated fat;
most often occurring in
manufactured products
Trans double bond (straight)
Although there are a few naturally occurring trans fats, such as in meat and FIGURE 18
dairy products, most trans fats come from industrial fat processing. This Cis and trans-fatty acids
takes an unsaturated fat (soft or liquid at room temperature) and bubbles

hydrogen ions through it until it’s solid at room temperature. This is known
as hydrogenation. HYDROGENATION
Adding hydrogen atoms to
There are two types of hydrogenation: full and partial. an unsaturated fatty acid
• Full hydrogenation makes a saturated fatty acid from a polyunsaturated

fatty acid.
• Partial hydrogenation makes a trans-fatty acid from a polyunsaturated fatty acid.
Polyunsaturated fats are normally reactive — they quickly oxidize and go
rancid, because other things such as oxygen can bond to their hydrocarbons.
But since hydrogenated fats are polyunsaturated fats that have been artificially
“filled up” with hydrogens, these fats now have a longer shelf life.
Naturally occurring trans fats emerge from biohydrogenation in the stomachs of
ruminant animals such as cows and sheep, as a defense against the toxic effects
of polyunsaturated fats on rumen bacteria. These include vaccenic acid (VA; 18
carbons long) and conjugated linoleic acid (CLA; specifically c9,t11-CLA).
While industrial hydrogenation is good for commercial food production, it’s
not so good for our body. This physical configuration changes how fats are
processed in our body.
For instance, eating a lot of artificially produced trans fats can:
• lower HDL;
ESSENTIAL FATTY ACID
• suppress the excretion of bile acids; Fatty acids that we need
• increase our own cholesterol production; for health and physiological
function include alpha-
• compete with essential fats for transport into the cells; and linolenic acid (ALA) and
• create and worsen essential fatty acid deficiencies. linolenic acid (LA)

Over time, this can add up to a higher risk of many chronic diseases. Even one
meal with a high trans fat content can diminish blood vessel function and elasticity.
In 2015, the United States Food and Drug Administration (FDA) concluded that
artificial trans fats in processed foods are not GRAS (generally recognized as safe)
and partially hydrogenated oils will need to be phased out of all food products.
Importantly, the few naturally occurring trans fats, such as conjugated linoleic CONJUGATED LINOLEIC
acid (CLA), which is formed in the rumens (multi-chambered stomachs) of ACID (CLA)
cows and sheep, don’t seem to harm us. They may even help us. As always, A type of naturally occurring
trans-fatty acid that may
eating minimally-processed whole foods is usually best.
have health benefits
Essential fatty acids: Omega-3 and omega-6 fatty acids

Just like there are essential amino acids that you need to get from your diet,
there are essential fatty acids that we need to consume in order to be healthy.
Essential fatty acids are two types of polyunsaturated fatty acids:
• α-linolenic acid (ALA), also notated as 18:3 n-3 (or 18:3 ω-3), which is an
omega-3 fatty acid (also called ω−3 fatty acids or n−3 fatty acids)
• linoleic acid (LA), also notated as 18:2 n-6 (or 18:2 ω-6), which is an
omega-6 fatty acid (also called ω−6 fatty acids or n−6 fatty acids)
Again, these fatty acids are by counting the carbons from the omega end
(methyl end) to the first double bond.
There are many forms of omega-3 and omega-6 fatty acids.
In mammals, the omega-6 fatty acid linoleic acid is considered the “parent”
omega-6 because it can be converted to other omega-6 fatty acids (such as
other forms of linoleic acid, eicosatriaenoic acid, and arachidonic acid [AA]).
Similarly, ALA is considered a “parent” omega-3. That’s because ALA has to be
converted to eicosapentaenoic acid (EPA; 20:5 ω-3) and docosahexaenoic acid
(DHA; 22: 6 ω-3).

Omega-3
double
bond
1 2 3 4 5 6 7 8 9 10
Omega end
Omega-6
double
bond
1 2 3 4 5 6 7 8 9 10
Omega end FIGURE 19

Omega-3 and omega-6
Hydrogen Carbon Oxygen
fatty acid structure
Omega-6 fatty acids Omega-3 fatty acids
Linoleic acid ɑ-Linolenic acid (ALA)

(18:2n-6) (18:3n-3)
Gamma linolenic acid (GLA) Steridonic acid (SDA)

(18:3n-6) (18:4n-3)
Dihomo gamma linolenic acid (DGLA) Eicosatraenoic acid (ETE)

(20:3n-6) (20:3n-3)
Arachidonic acid (AA) Eicosapentaenoic acid (EPA)

(20:4n-6) (20:5n-6)
FIGURE 20
Docosatetraenoic acid Docosahexaenoic acid (DHA) Conversion of omega-6 and
(22:4n-6) (22:6n-6) omega-3 fatty acids

Omega-3 fatty acids

The most important omega-3 fatty acids for us are α-linolenic acid (ALA),
docosahexaenoic acid (DHA), and eicosapentaenoic acid (EPA).
• Plant sources such as flax, chia, hemp, and walnuts are rich in ALA.
• Marine sources such as fatty cold-water fish (and fish oil) and algae (the
original omega-3 sources for fish) are rich in EPA and DHA, which are
widely recognized as the most beneficial omega-3 fats.
• Human breast milk is also an important source of EPA and DHA for
developing infants.
We don’t convert ALA to EPA / DHA very well, so wherever possible, look for
direct dietary sources of EPA / DHA.
As we’ve seen, cell membranes are fat-based. One reason omega-3 fats are so
important is that they keep our cells’ membranes more “fluid”, which provides
several benefits.
For example:
• When brain cell membranes are relatively fluid, messages from
neurochemicals such as serotonin can be transmitted more easily. Getting
enough EPA / DHA early in life helps with brain development; getting it later
in life helps prevent or slow neurodegenerative disorders.
• When muscle cell membranes are more fluid, it increases insulin sensitivity.
These essential fats also play a role in many other areas, including
cardiovascular function, nervous system function, and immune health.
Eicosanoids are signaling molecules that help regulate processes such as EICOSANOIDS
immunity or inflammation. Both omega-3 and omega-6 intake can affect Signaling molecules that help
regulate processes such as
eicosanoid production.
immunity or inflammation
Omega-3 fats are considered anti-inflammatory. They tend to promote
eicosanoids that do things like:
• dilate (open up) our blood vessels to improve blood flow;
• lower inflammation;
• prevent blood coagulation and clumping;
• decrease pain;
• dilate our airway; and
• support our immune system.

Omega-6 fatty acids

Three key omega-6 fatty acids are:
• linoleic acid (LA);
• gamma-linolenic acid (GLA); and
• arachidonic acid (AA).
Omega-6s are considered pro-inflammatory. They promote eicosanoids that do
the opposite of omega-3 eicosanoids, such as:
• constrict blood vessels;
• increase inflammation;
• cause blood clotting;
• increase pain; and
• constrict our airway.
These processes may sound unhealthy, but we need them. Without them, we
couldn’t heal from injuries or recover from training sessions.
Our genes may also affect fat metabolism, including unsaturated fats.
The omega-3 index • Below 4% on the omega-3 index

= High risk
If you want to get really fancy and determine
• Between 4-8% = Intermediate risk
the exact amount of omega-3 fatty acids
that are best for you, consider testing your • Over 8% = Low risk
omega-3 index. Find yourself in risky territory and want to
The omega-3 index is the percent of EPA and increase your omega-3 index? That’s easy:
DHA combined in the membranes of your Eat more omega-3 rich fish. Or take a fish oil
red blood cells. This measure gives a picture supplement.
of your overall omega-3 status; the fluidity of Of course, the results of eating EPA and
your cell membranes; and your potential risk DHA on your omega-3 index will depend
for sudden cardiac death. For example: on certain physical factors, like your body

weight, age, sex, physical activity level, and How much of an index increase is even
starting omega-3 index. possible? One study found that consuming
1.8 grams of EPA and DHA (combined) each
For example, an older woman with a low
day for 5 months could boost a person’s
body weight, low starting omega-3 index, and
omega-3 index by over 5%.
a high physical activity level would see the
greatest increase in her omega-3 index by
eating more EPA and DHA.
Triglycerides
Triglyceride synthesis
Built from three fatty acids plus a glycerol backbone, triglycerides (tri = “three”)
are the storage form of lipids in humans. Similarly, diglycerides (diacylglycerols)
have two fatty acids, while monoglycerides (monoacylglycerol) have one fatty
acid attached to a glycerol backbone.
Short-chain
fatty acid Glycerol
Triglyceride
Medium-chain
(3 fatty acids + glycerol)
fatty acid
Long-chain
fatty acid
Even though glycerol is the same in every triglyceride molecule, the fatty FIGURE 21
acids can be short or long; they can be all saturated, all unsaturated, or any Triglyceride structure
combination. Because of the different possible fatty acids, triglycerides can exist
as a fat (solid) or oil (liquid) at room temperature.
Lipolysis
Triglycerides are stored in adipocytes (fat cells) in the body. About 95% of our
dietary fat is also in the form of triglycerides.
LIPOLYSIS
During the process of lipolysis, triglycerides are broken down into their The breakdown of
individual fatty acids (plus a free glycerol, or two free fatty acids and a triglycerides into fatty acids
and glycerol
monoglyceride). Lipolysis often happens during digestion, or when we need to

retrieve stored body fat for fuel. Conversely, during the process of triglyceride TRIGLYCERIDE SYNTHESIS
synthesis, fatty acids are packaged into triglycerides for transport or storage. The formation of triglycerides
from fatty acids and glycerol
FIGURE 22
Triglyceride synthesis Triglyceride synthesis

and lipolysis
Short-chain
fatty acid Glycerol
Triglyceride
Medium-chain
(3 fatty acids + glycerol)
fatty acid
Long-chain
fatty acid AMPHIPATHIC
Being both hydrophilic and
hydrophobic, as in the case
of phospholipids that make
up cell membranes
Lipolysis
MICELLE
Lipid molecules that arrange
Phospholipids and sterols themselves in a spherical
form in aqueous solutions
Phospholipids are lipids (diglycerides) with a phosphate group attached (PO4).
Phospholipids are special because they are amphipathic (both hydrophilic and
PHOSPHOLIPID BILAYER
hydrophobic). When phospholipids are arranged with their fatty acid “tails” A double-layered formation
positioned against each other and the phosphate “heads” on the outside, it of phospholipids that
creates either a single layer micelle or a double layer (bilayer). Our cells use provides the basis for cell
this phospholipid bilayer to form their membranes — semi-permeable barriers membranes
that regulate what gets in and out of the cell and the structures, known as
organelles, inside it. ORGANELLES
Structures inside cells with
particular functions

Carbohydrate chain
Membrane
receptor Protein
Glycoprotein (glycan)
Channel
Outside of cell
Phospholipid
bilayer
Cholesterol
Inside of cell
Hydrophilic head
Hydrophobic tail
Phospholipid
Sterols are yet another class of lipid; they’re the most structurally different FIGURE 23
compared to the others. Sterols have a steroid nucleus (a center with 4 Structure of a cell
separate carbon rings) and a hydroxyl group. membrane
Plant sterols (aka phytosterols) also likely play a key role in health and function
(particularly in lowering our risk of cardiovascular disease). We also make a
variety of types of sterols in our bodies, such as: PHYTOSTEROLS
• cholesterol; Plant-based sterol
compounds with
• bile acids; and potential health benefits;
phytoestrogens are an
• steroid hormones (such as our sex hormones and corticosteroids) example
We’ll go into cholesterol a bit more when we discuss lipoproteins later in this
section. STEROID HORMONES
A large group of sterol-based
hormones, primarily our sex
hormones (e.g., estrogen,
testosterone) and corticoid
hormones (e.g., cortisol)

Fat digestion, absorption, metabolism,

and transport
A key part of fat digestion is the body using lipases, or fat-digesting enzymes, LIPASES
breaking down triglycerides into fatty acids and glycerol, which are repackaged Fat-digesting enzyme
in various ways before entering the bloodstream.
The mouth
Fat digestion in the mouth includes chewing the food to make it smaller and
mixing in a lingual lipase that is stable in acidic environments.
The stomach
A little digestion of fats occurs in the stomach, mostly the breaking apart of
proteins attached to fats (i.e., lipid-protein complexes like lipoproteins).
Lingual lipase from the mouth continues to work, while gastric lipase is
secreted by the chief cells of the stomach. About 10 to 30% of triglyceride
digestion happens in the stomach, with most of fat digestion happening in the
small intestine.
While in the stomach, fat is churned and smushed, which emulsifies the
smaller fat droplets. Emulsification is a way of holding fat stable in a water- EMULSIFICATION
based suspension by making the fat droplets very small, then mixing them Holding fat stable in a water-
rapidly. (In daily life, you might recognize cream, salad dressing, or mayonnaise based suspension by making
the fat droplets very small,
as emulsions.) Emulsification divides the fat into small droplets that offer more
then mixing them rapidly
surface area to digestive enzymes than the original larger triglyceride droplet.
The small intestine

Fat digestion takes place mostly in the small intestine, where bile salts continue
to emulsify the triglycerides in the food we’ve eaten.
The pancreas secretes pancreatic lipase, the major enzyme of triglyceride
digestion, into the small intestine, specifically the duodenum, where it
hydrolyzes (breaks apart) the triglycerides and removes the fatty acids from
their glycerol backbone.
Generally, only a small percentage of triglycerides have all three fatty acids
removed. Most end up as a monoglyceride (glycerol + one fatty acid).
(Fun fact: Orlistat, a drug developed to treat obesity, inhibits pancreatic lipase,
which leads to incomplete digestion of triglycerides. This decreases fat absorbed

by 30% and increases fat excreted. That works out to about 200 kcal less from
fat a day. Side effects are basically whatever you can imagine happening with
undigested fat shooting through your intestines.)
After they are broken down, fatty acids and glycerol are absorbed by the
GLYCOLYSIS
intestinal cells (enterocytes). In the enterocyte, glycerol is either converted to
A process that creates ATP
ɑ-glycerophosphate that can be used for energy (via the process of glycolysis) from glycogen, glucose, and
or it is reformed into a triglyceride. glycerol
The enterocytes, or intestinal cells, can absorb small particles of fat, then
convert the fat particles, and repackaging them into lipoproteins called
chylomicrons. CHYLOMICRONS
Lipoproteins that transport
Once in chylomicron format, these particles enter the intestinal lymphatic fats from the small intestine
vessels, called lacteals, effectively bypassing the portal circulation. All lymphatic to the liver
fluid in the body, and the chylomicrons in it, eventually rejoin the general
(systemic) circulation, and chylomicrons eventually get picked up by the liver.
Then, the liver can do more repackaging work, converting fatty acids into
triglycerides or releasing them into circulation as other types of lipoproteins.
Generally, the liver is very effective at metabolizing dietary fats. However, when
people consistently eat more energy than they need, and carry much more
body fat than is optimal for them physiologically, we often see a build-up of fats
in the liver, a condition known as hepatic steatosis or non-alcoholic fatty liver
disease (NAFLD). (Excess body fat can also build up in other tissues, such as NON-ALCOHOLIC FATTY
LIVER DISEASE (NAFLD)
the heart, muscles, or kidneys.)
Aka hepatic steatosis, a
Fatty liver is one of the hallmarks of metabolic syndrome, and one of the buildup of fat in the liver,
reasons why maintaining a healthy body composition is so important. usually due to a poor diet,
metabolic syndrome, or
Because it takes a long time to break down and transport, fat enters the blood other non-alcohol-related
several hours after we’ve eaten it. Packaged triglycerides circulating in the blood causes
(carried by chylomicrons) are again broken down into free fatty acids and glycerol
with the help of an enzyme called lipoprotein lipase. This occurs so they can LIPOPROTEIN LIPASE
pass through yet another cell membrane and into the tissues of our body. An enzyme that breaks
down lipoproteins
Once through the membrane, they’re either:
• oxidized (through the process of ß-oxidation/fat-oxidation) and used to
ß-OXIDATION
transfer energy in skeletal muscle or other tissues; or
The oxidation (“burning”)
• converted back (again) into triglycerides for storage in adipose tissue, of fat that allows for energy
skeletal muscle, etc. release, aka fat oxidation

Cholesterol level of lipoproteins that carry cholesterol and

triglycerides.
and lipoproteins All lipoproteins are not created equal.
You may be worried about your “cholesterol
We have several types of lipoproteins that
levels”, or whether you’re getting too much
carry fats around in the body. These vary by
cholesterol in your diet.
size and density. These differences affect how
Cholesterol is an essential molecule they work in the body, and whether they pose
in the body. a risk to us in the wrong amounts.
We need cholesterol for making our cell • Chylomicrons carry fats from the small
membranes as well as other structures such intestine to the liver. They’re the largest,
as hormones. So, cholesterol is not a bad and contain much more triglyceride than
thing in and of itself. cholesterol.
In fact, most of the cholesterol in circulation • Very low-density lipoproteins (VLDLs) are
is made by the liver, and it doesn’t come from packaged in the liver to be sent elsewhere
the foods we eat. The form of cholesterol in, in the body.
say, an egg is not well absorbed in our gut.
• Low-density lipoproteins (LDLs) carry
Cholesterol production is carefully controlled what people often call “bad” cholesterol,
by feedback mechanisms in the body, and because they travel in the bloodstream,
isn’t significantly affected by the cholesterol carry fat to our cells, and can oxidize in
we eat, although there is a strong genetic blood vessels, forming plaques that can
component to cholesterol levels. So, if you lead to heart disease. We need them, but
have high cholesterol, it may not be from don’t want too much cholesterol in them.
your daily omelet; rather, it may be your
• High-density lipoproteins (HDLs) are
parents’ fault.
the smallest particles, and contain the
However, as with other types of fats, most cholesterol relative to triglyceride.
cholesterol can’t travel on its own through the They carry what’s often thought of as
water-based bloodstream. It needs to hitch a “good cholesterol”. Generally, we want
ride on lipoproteins. the cholesterol in these particles to be a
little higher, as they’re like the “cholesterol
A “cholesterol test” or “lipid profile” that our
cleanup crew” that shuttles cholesterol
doctor might ask us to do mostly tests our
back to the liver for recycling.

Protein
Phospholipid
membrane
Triglyceride
Cholesterol
Chylomicron Very low-density Low-density High-density

lipoprotein (VLDL) lipoprotein (LDL) lipoprotein (HDL)
LDL and cardiovascular disease vegetables, nuts and seeds, fish and other
lean proteins, whole grains, beans, and
Despite what the internet says, LDL
legumes) tend to improve it.
particles (specifically LDL-ApoB100) are
a key component in atherosclerosis and We’ll look more at specific types of dietary
cardiovascular disease. Dietary trans-fats fats and nutritional recommendations later, in
and saturated fats (particularly palmitate) Units 2 and 3.
increase blood LDL particles, while dietary How could you apply this to your own
cholesterol does not increase LDL particles or experience?
the risk of cardiovascular disease.
We can easily measure lipoprotein levels and
We can affect our lipoprotein profile with their cholesterol count with a simple blood
diet. test. This can tell us about the effects of a
While each person’s individual response particular dietary pattern.
to a given diet will vary, there seem to be For instance, if you switch from a high-
some trends. carbohydrate, low-fat diet to a low-
In general, for most people: carbohydrate, high-fat diet (or vice versa),
you can have a lipid profile taken to see if
• Eating more omega-3 polyunsaturated
there have been any changes.
fatty acids seems to lower LDL cholesterol
and increase HDL cholesterol. Lipoprotein levels and their cholesterol count
can change rapidly, and even a month on a
• Eating more saturated fat seems to raise
new diet is enough to show a difference.
LDL cholesterol and triglycerides.
If you’re not an MD, you can collaborate with
• Diets high in processed foods tend to
your health care provider to interpret the lab
worsen our lipoprotein profile.
tests. These diagnostic data may help you
• Conversely, diets with lots of minimally- decide whether a particular nutrition plan is
processed whole foods (e.g., fruits, taking you in the right direction.

Why are dietary fats important? CHYLOMICRONS

A type of lipoprotein (the
largest type) that carry fats
Dietary fat has six major roles: from the intestines to other
parts of the body
1. It provides us with energy (indeed, it’s the most energy-dense macronutrient).
2. It helps make and balance hormones, particularly our steroid hormones
(such as sex hormones and corticosteroid hormones). VERY LOW-DENSITY
LIPOPROTEINS (VLDLS)
3. It forms our cell membranes.
A large lipoprotein made
4. It forms our brains and nervous systems. in the liver that carries
triglycerides to our cells
5. It helps transport the fat-soluble vitamins A, D, E, and K.
6. It gives us two fatty acids that we can’t make on our own:
a. linoleic acid (an omega-6 fatty acid), and LOW-DENSITY
LIPOPROTEINS (LDLS)
b. linolenic acid (an omega-3 fatty acid).
A type of lipoprotein that
While it’s important to learn about the specific features of each fat type, keep carries fats to our cells; can
the big picture in mind. cause plaque leading to
heart disease, often called
Focus on these key points: “bad” cholesterol
• Humans evolved eating a varied and seasonal diet. We thrive best on a mix
of fat types that occur naturally in different types of foods.
HIGH-DENSITY
• We want a relatively equally balanced mix of fat types. LIPOPROTEINS (HDLS)
A type of lipoprotein that
• This balance comes naturally if we choose a wide selection of diverse, shuttles cholesterol back to
whole, minimally-processed foods, such as: the liver for recycling; acts
• nuts and seeds as the “cholesterol cleanup
crew”; often called “good
• avocados
cholesterol”
• dairy
• eggs
• fatty fish
FAT-SOLUBLE VITAMINS
• beef, pork, and lamb
Vitamins (such as A, D, E,
• poultry and K) that cannot dissolve
• wild game in water, and require fat for
• tofu and tempeh transport and absorption
• olives and extra-virgin olive oil
• Fish and animal products that are wild-caught or pasture-raised will usually
have the best fatty acid profiles (of course, these may not always be
available, practical, and/or affordable).
• Try to minimize or eliminate refined and processed foods containing
industrially produced fats and artificially hydrogenated fats.

• At times, it may be useful to supplement particular fat types, especially

omega-3s (e.g., fish, krill, or algae oil).
• Match your nutrition plan to your (or your clients’) unique body, preferences,
and needs.
How much fat do you need?

As always, the answer is: It depends.
In Unit 2, we’ll look at calculating fat intake based on activity, using this rough
guideline:
How much fat do people likely need?
SUGGESTED FAT INTAKE*
Lightly active ~0.3-0.5 g of fat per lb of bodyweight (~0.65-1.1 g/kg)

Moderately active ~0.5-0.7 g/lb (~1.1-1.5 g/kg)
Highly active ~0.7-0.9 g/lb (~1.5-2 g/kg)
* Note: Fat intake could be as low as 0.2 g/lb (0.4 g/kg) on low-fat diets, or as high as 2.0 g/lb (4.4 g/kg) for ultra-endurance
athletes on ketogenic diets.
In terms of specific fat / lipid types, here are the current recommendations
for Adequate Intake (AI) for essential fats, and guidelines for cholesterol and
saturated fat intake:
How much fat do people likely need?
LINOLEIC ACID α-LINOLENIC

(OMEGA-6) ACID (OMEGA-3) CHOLESTEROL SATURATED FAT TRANS FAT
% OF DAILY
(GRAMS/DAY) MILLIGRAMS/DAY CALORIES GRAMS/DAY
Men 19-50 years 17 1.6

no
Women 19-50 years 12 1.1
specific
<10 0
Men > 50 years 14 1.6 recommenda-
tions2
Women > 50 years 11 1.1
2 Under 300 mg / day was the recommendation that appeared in Thompson TG, Veneman AM. Dietary guidelines for Americans 2005. United
States Department of Health and Human Services and United States Department of Agriculture. 2005.

35
+31
30
25
Change in total mortality (%)
20
15
10 +9
5
-10 -19
0
-5
-10
-15
-20
Trans fat Saturated fat Monounsaturated fat Polyunsaturated fat
Figure adapted from: O’Keefe JH, DiNicolantonio JJ, Sigurdsson AF, Ros E. Evidence, not evangelism, for dietary
recommendations. Mayo Clinic Proceedings 2018 Feb 1 (Vol. 93, No. 2, pp. 138-144).
In summary FIGURE 24
Estimated effects of
substituting various
This is a relatively brief overview of the science of the three major types of dietary fat for
macronutrients: protein, carbohydrates, and fat. carbohydrate on total
mortality
Obviously, there’s a lot to learn, and more that we still don’t know. Nutritional
science is dynamic, always-evolving, and mind-bogglingly complex. (For
more on this, see: Why Nutrition Science Is So Confusing.)
Keep this in mind when you run across a diet that focuses on one
macronutrient, or one component of the metabolism of a macronutrient.
In Units 2 and 3, we’ll move from the theoretical to the practical to look at:
• how to calculate macros (and energy intake); and
• how to put those calculations into practice with a macronutrient-based plan.

01 ScienceOfMacros

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DE F I N IT IIVE

• We’ll provide an introduction to the science of

• What are macronutrients?

• What is a macronutrient ratio, or split?

• What’s the role of energy (i.e., calories) and energy

• For each group of macronutrients, we’ll explain:

• their structure and function;

• similarities and differences among the molecules in each

• what those nutrients do in our bodies.

• We’ll show how knowing the nutritional science helps us

UNIT 1: The science of macronutrients | 2

What are macronutrients?

While macronutrients are important, they aren’t the only factors

UNIT 1: The science of macronutrients | 3

• Macronutrients vary a lot in their makeup. For instance, the family

What is a macronutrient ratio?

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Food quality also matters.

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What is the role of energy?

Energy balance strongly affects our health, body composition,

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Factors that influence Factors that influence

Appetite Energy burned at rest

and so on); The ratio of lean mass (such

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Energy balance can also affect physiological function, performance,

Because energy balance is so important physiologically, our bodies have

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When planning a macronutrient-based program:

Each macronutrient stores a different amount of energy.

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Regardless of how energy is measured, what matters most is:

• 1 gram of protein = 5.65 kcal

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In the real world, calculating energy needs, intake, and use is

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100 Predicted bodyweight

As you can see: FIGURE 4

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We’ll look more at tailored energy and macronutrient calculations

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Our bodies are always building up and breaking down proteins.

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Nutrition nerd stuff

The role of proteins • Inhibition of autophagy (cellular waste

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possibly fetal programming of postnatal • Digestive function

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Amino acids PEPTIDES

H molecule (as well as other

Amino group (NH2)

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Categorizing amino acids NON-ESSENTIAL AMINO

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Nutrition nerd stuff

Branched chain amino • a chemical signal (such as the presence

protein synthesis • a mechanical signal (such as exercise).

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Stereoisomers: The same but different INSULIN