PROTEINS

 A large complex molecules that play many critical roles in the body. They do most of the work in
cells and are required for structure, function, and regulation of the tissues and organs.

Proteins were first recognized as a distinct class of biological molecules in the 18th century,
distinguished by their ability to coagulate or flocculate under heat or acid treatments. They were first
described by Gerardus Johannes Mulder and named by Jöns Jacob Berzelius in 1838. Early nutritional
scientists believed that protein was the most important nutrient for maintaining the body's structure,
and the term "protein" was derived from the Greek word "proteios". Early studies focused on proteins
that could be purified in large quantities, such as blood, egg whites, toxins, and digestive/metabolic
enzymes. Linus Pauling predicted regular protein secondary structures based on hydrogen bonding,
while Walter Kauzmann contributed to understanding protein folding and structure mediated by
hydrophobic interactions. The first protein to be sequenced was insulin, and the first protein structures
to be solved were hemoglobin and myoglobin.

Amino acids are classified into two groups:

-Essential amino acids

- Nonessential amino acids

ESSENTIAL AMINO ACIDS

 Essential amino acids cannot be made

by the body. As a result, they must come from food. The 9 essential amino acids are: histidine,
isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, and valine.

Histidine:

 Histidine helps make a brain chemical (neurotransmitter) called histamine. Histamine plays an
important role in your body’s immune function, digestion, sleep and sexual function.

Isoleucine:

 Isoleucine is involved with your body’s muscle metabolism and immune function. It also helps
your body make hemoglobin and regulate energy.

Leucine:

 Leucine helps your body make protein and growth hormones. It also helps grow and repair
muscle tissue, heal wounds and regulate blood sugar levels.

Lysine:

 Lysine is involved in the production of hormones and energy. It’s also important for calcium and
immune function.
Methionine:

 Methionine helps with your body’s tissue growth, metabolism and detoxification. Methionine
also helps with the absorption of essential minerals, including zinc and selenium.

Phenylalanine:

 Phenylalanine is needed for the production of your brain’s chemical messengers, including
dopamine, epinephrine and norepinephrine. It’s also important for the production of other
amino acids.

Threonine:

 Threonine plays an important role in collagen and elastin. These proteins provide structure to
your skin and connective tissue. They also help with forming blood clots, which help prevent
bleeding. Threonine plays an important role in fat metabolism and your immune function, too.

Tryptophan:

 Tryptophan helps maintain your body’s correct nitrogen balance. It also helps make a brain
chemical (neurotransmitter) called serotonin. Serotonin regulates your mood, appetite and
sleep.

Valine:

 Valine is involved in muscle growth, tissue regeneration and making energy.

NONESSENTIAL AMINO ACIDS

 means that our bodies can produce the amino acid, even if we do not get it from the food we
eat. Nonessential amino acids are: alanine, arginine, asparagine, aspartic acid, cysteine, glutamic
acid, glutamine, glycine, proline, serine, and tyrosine.

Glutamine

 is one of the most common amino acids in the body. Glutamine protects the stomach and
gastrointestinal tract. In particular, glutamine is used to produce energy for the gastrointestinal
tract. Glutamine promotes the metabolization of alcohol to protect the liver.

Aspartate

 is one of the amino acids that is most usable for energy. Aspartate is one of the amino acids
positioned most closely to the tricarboxylic acid (TCA) cycle in the body that produces energy.
The TCA cycle is like the engine that powers cars. Each cell in our bodies functions to produce
energy.

Glutamate
  Glutamic acid is an amino acid used to form proteins. In the body, it turns into glutamate. This is
a chemical that helps nerve cells in the brain send and receive information from other cells. It
may be involved in learning and memory.

Arginine

 Arginine plays an important role in opening up the veins to enhance blood flow. Nitric oxide that
opens up the veins is made from arginine. Arginine is a useful amino acid for removing excess
ammonia from the body. Arginine increases immunity.

Alanine

 Alanine supports function of the liver. Alanine is used to make glucose that are needed by the
body. Alanine improves the metabolization of alcohol.

Proline

 Proline is one of the amino acids contained in collagen that makes up skin tissue. Proline is one
of the most important amino acids to the natural moisturizing factor (NMF) that keeps skin
moist.

Cysteine

 Cysteine reduces the amount of black melanin pigmentation made. Cysteine is plentiful in head
hair and body hair. Cysteine increases the amount of yellow melanin made instead of black
melanin.

Asparagine

 An amino acid that was discovered from asparagus. Both asparagine and Aspartate are
positioned close to the tricarboxylic acid (TCA) cycle that produces energy.

Serine

 An amino acid used to make phospholipids and glyceric acid.

Glycine

 A non-essential amino acid that is made in the body. Glycine is plentiful in the body. It acts as a
transmitter in the central nervous system and helps regulate body functions such as locomotion
and sensory perception. Glycine makes up one-third of collagen.

Tyrosine

 Tyrosine is used to make many types of useful amines. Tyrosine is grouped as an aromatic amino
acid together with phenylalanine and tryptophan.
The way in which a protein coils to form a precise three-dimensional (3D) shape is called its TERTIARY
STRUCTURE

 Tertiary structure: the overall shape of a single protein molecule; the spatial relationship of the
secondary structures to one another.
 Four types of bonds help proteins maintain their tertiary structures: Hydrogen bonds - formed
between strongly polar groups like -NH-, -CO-, and -OH. Broken by changes in temperature or
change in pH • •
 Disulfide bonds - formed between two cysteine molecules which contain sulfur atoms. Can be
broken by reducing agents
 lonic bonds - formed between ionized amine (NH₂ + ) and ionized carboxylic acid (COO) groups.
They can be broken by pH changes
 Hydrophobic interactions - form between non-polar side group

CLASSIFICATION OF PROTEIN

FIBROUS PROTEINS

 -When polypeptide chains run parrallel and are held together by hydrogen and disulfide bonds,
then the fiber-like structured is formed. Such proteins are generally insoluble in water. These
are water-insoluble proteins.
 Example: keratin (present in hair, wools, and silk) and myosin(present in muscles), and etc.

GLOBULAR PROTEINS

 These structure result when the chains of polypeptide coil around to give a spherical shape.
These are usually soluble in water.

 Example: Insulin and albunmins are common examples of globular protein

PROTEIN FUNCTION

Enzymes

 are proteins that help speed up chemical reactions in our bodies. Enzymes are essential for
digestion, liver function and much more. Too much or too little of a certain enzyme can cause
health problems. Enzymes in our blood can also help healthcare providers check for injuries and
diseases.

Structural proteins

 are a category of proteins responsible for functions ranging from cell shape and movement to
providing support to major structures such as bones, cartilage, hair, and muscles. This group
includes proteins such as collagen, actin, myosin, and keratin.
Transport proteins

 are proteins that transport substances across biological membranes. Transport proteins are
found within the membrane itself, where they form a channel, or a carrying mechanism, to
allow their substrate to pass from one side to the other.

 The substances transported by these proteins can include ions such as sodium and potassium;
sugars such as glucose; proteins and messenger molecules; and many more.

AntibodIes

 is a protein component of the immune system that circulates in the blood, recognizes foreign
substances like bacteria and viruses, and neutralizes them. After exposure to a foreign
substance, called an antigen, antibodies continue to circulate in the blood, providing protection
against future exposures to that antigen.

Hormones

 Protein hormones are also known as peptide hormones. The hormonal response in the human
body is slow as compared to that of the nervous system. The hormones act on the hormone
receptors. The hormones help in regulating, activating, and inhibiting the physiological
processes.

PROTEIN STRUCTURE AND FUNCTION RELATIONSHIP

Amino acid sequence determines protein structure and structure dictates biochemical function, proteins
that share a similar amino acid sequence usually perform similar biochemical functions, even when they
are found in distantly related organisms.

TYPES FUNCTION EXAMPLE

Enzymatic Enzymatic Example:
protein aids • Lipases: This group of enzymes help digest fats
 your digestive in the gut.
system by • Amylase: In the saliva, amylase helps change
accelerating the starches into sugars.
metabolic • Maltase: This also occurs in the saliva, and
processes breaks the sugar maltos into glucose.
occurring within
your cells.
Transport Transport Example:
protein carry a Hemoglobin - contains iron, which allows it to pick up
vital materials oxygen from the air we breathe and deliver it
to the cells. everywhere in the body. You can think of hemoglobin
as the iron ("heme"), oxygen transport protein,
("globin") found in red blood cells.
carrier protein-is a type of protein that transports a
specific substance through intracellular
compartments, into the extracellular fluid, or across
cells.
Channel proteins -are a type of facilitated diffusion
where molecules are moved across the membrane
through a protein, without using energy.

Structural Structural Collagen is protein molecules made up of amino

protein is acids. It provides structural support to the
fibrous in that it extracellular space of connective tissues
creates the
framework
necessary for
healthy bones,
tendons, skins,
and cartilage
Contractile Contractile Examples:
protein also Myosin- a major component of the contractile unit of
known as motor a muscle cell. Myosin is a superfamily of proteins that
proteins, the play an important role in binding actin, hydrolyzing
purpose is to ATP and transducing force.
regulate the Kinesin-molecular motor proteins are responsible for
movement of many of the major microtubule-dependent transport
your heart and pathways in neuronal and non-neuronal cells.
muscles.
Hormones Hormonal Examples
 protein enables Insulin is a protein hormone produced by the
the cells in your pancreas. Basically, insulin is the protein that draws
body to sugar out of your bloodstream and into your cells for
communicate energy.
with each other. Prolactin -is a protein hormone that is stored by the
pituitary gland also known as lactotropin. It is a
protein best known to enable mammals, usually
females, to produce milk.

Defensive Defensive Examples

protein keep defense proteins include antibodies, lectins, and
your immune antiviral proteins. They are critical components of the
system strong immune system, allowing our bodies to fight off
and helps infections and stay healthy. Antibodies are proteins
defend against that protect you when an unwanted substance enters
diseases and your body.
infections. Lectins are a class of proteins responsible for several
biological roles such as cell-cell interactions, signaling
pathways, and several innate immune responses
against pathogens

Storage -is responsible Examples

for storing Ferritin, an iron storage protein, is the primary iron
mineral ions. storage mechanism and is critical to iron homeostasis.
Ferritin makes iron available for critical cellular
processes while protecting lipids, DNA, and proteins
from the potentially toxic effects of iron.
Casein-stores amino acids, mainly used for muscle
support and growth. It has a large influence on
suppressing protein breakdowns and is often used in
protein supplements.

PROTEIN SYNTHESIS

 Protein synthesis is the creation of proteins. In biological systems, it is carried out inside the
cell. In prokaryotes, it occurs in the cytoplasm. In eukaryotes, it initially occurs in the nucleus to
create a transcript (mRNA) of the coding region of the DNA.
  Protein synthesis is the process in which cells make proteins. It occurs in two stages:
transcription and translation. Transcription is the transfer of genetic instructions in DNA to
mRNA in the nucleus.
 The first step is transcription in which the sequence of one gene is replicated in an RNA
molecule.
 The second step is translation in which the RNA molecule serves as a code for the formation of
an amino-acid chain (a polypeptide)

PROTEIN SOURCES

 Animal-based foods (meat, poultry, fish, eggs, and dairy foods) tend to be good sources of
complete protein, while plant-based foods (fruits, vegetables, grains, nuts, and seeds) often lack
one or more essential amino acid.

PROTEIN DENATURATION

 in biology, process modifying the molecular structure of a protein. Denaturation involves the
breaking of many of the weak linkages, or bonds (e.g., hydrogen bonds), within a protein
molecule that are responsible for the highly ordered structure of the protein in its natural
(native) state. Denatured proteins have a looser, more random structure; most are insoluble.
Denaturation can be brought about in various ways—e.g., by heating, by treatment with alkali,
acid, urea, or detergents, and by vigorous shaking

CAUSES AND CONSEQUENCES OF PROTEIN DENATURATION

Proteins become denatured due to some sort of external stress, such as exposure to acids, bases,
inorganic salts, solvents, or heat. Some proteins can regain their lost structure after they're denatured;
this is a process called renaturation.

PROTEIN RELATED DISEASES

Alzheimer's disease is the most common type of dementia. It is a progressive disease beginning with
mild memory loss and possibly leading to loss of the ability to carry on a conversation and respond to
the environment. Alzheimer's disease involves parts of the brain that control thought, memory, and
language.

PARKINSON'S DISEASE a progressive disease of the nervous system marked by tremor, muscular rigidity,
and slow, imprecise movement, chiefly affecting middle-aged and elderly people. It is associated with
degeneration of the basal ganglia of the brain and a deficiency of the neurotransmitter dopamine.

HUNTINGTON'S DISEASE an inherited disorder that causes nerve cells (neurons) in parts of the brain to
gradually break down and die. The disease attacks areas of the brain that help to control voluntary
(intentional) movement, as well as other areas.

Creutzfeldt-Jakob disease (CJD) is a rapidly progressive, invariably fatal neurodegenerative disorder

believed to be caused by an abnormal isoform of a cellular glycoprotein known as the prion protein.
CYSTIC FIBROSIS a genetic condition that affects a protein in the body. People who have cystic fibrosis
have a faulty protein that affects the body's cells, tissues, and the glands that make mucus and sweat

GAUCHER'S DISEASE a rare genetic disorder passed down from parents to children (inherited). When
you have Gaucher disease, you are missing an enzyme that breaks down fatty substances called lipids.
Lipids start to build up in certain organs such as your spleen and liver.