Proteins

Multipurpose

molecules

2006-2007
Protein
 Protein is the most abundant nitrogen-containing
compound in the diet and the body.
 Made up of chains of amino acids. It is one of the five

classes of complex biomolecules present in cells and

tissues, the others being DNA, RNA, polysaccharides, and
lipids.
 The sequence of amino acids is determined by DNA. Amino

acids are composed of carbon, hydrogen, oxygen, nitrogen

and sometimes sulfur.
Proteins
 Most structurally & functionally diverse group of
biomolecules
 Function:
involved in almost everything
Metabolism
Support
Transport
Regulation
Motion
Metabolism
Enzymes
Biological catalysts – speed up chemical reactions
 Digestive enzymes aid in hydrolysis
o Lipase
o Amylase
o Lactase
o Protease
 Molecular Biology
o Polymerase
o Ligase
 Industry
o Dairy, baby food, rubber, beer, photography, contact lense
cleaner
Support
Structural proteins
Keratin – hair and nails
Collagen – supports ligaments, tendons, and skin
Silk – cocoons and spider webs
 Transport
Channel and carrier proteins in the cell membrane
Allows substances to enter and exit the cell
Transport molecules in blood
Hemoglobin – transports oxygen in the blood
Defense
Antibodies
Combat bacteria and viruses
Regulation
Hormones
Intercellular messengers that influence metabolism
Insulin – regulates the amount of glucose in the
blood and in cells
Human growth hormone – its presence determines
the height of an individual
Receptor Proteins
Built into the membranes of nerve cells
Detect chemical signals (neurotransmitters)
released by other nerve cells
Motion
Muscle contraction
Actin and myosin – make up muscle fibers
Motor proteins within the cell
Allow cell components to move from place to place
Flagella- move the cell
Cilia- move contents around the cell
 Proteins
 Structure:
monomer = amino acids
20 different amino acids
12 made by body
8 essential amino acids (must get from food)
polymer = polypeptide
protein can be one or more polypeptide chains
folded & bonded together
large & complex molecules
complex 3-D shape
hemoglobin

Rubisco growth
hormones
Amino acids
 Structure:

central carbon (α carbon)

amino group

carboxyl group (acid)

R group (side chain)
 variable group H O
 confers unique H ||
|
chemical properties
—N—
of the amino acid —C— C—OH
H |
R
Classification of amino acids
Sulfur containing amino acids
 Form disulfide bridges
 cross links betweens sulfurs in amino acids

H-S
H-S –– S-H
S-H

You wondered

why perms

smelled like

rotten eggs?
Amino Acid Absorption

 Amino acids are absorbed in the small intestine

 Amino acids are transported to the liver from the intestines

via the portal vein

 In the liver, amino acids are

• Used to synthesize new proteins

• Converted to energy, glucose, or fat

• Released to the bloodstream and transported to cells

throughout the body

Amino acid status
When your body exceeds the number of amino acids
that are being broken down, you are in what’s
considered to be a ‘positive amino-acid balance’ also
known as a muscle-building or anabolic state

. When the number of amino acids being broken

down, exceeds the number of amino acids being
created, you are in what is considered a breakdown of
muscle mass, or a catabolic state.
 Energy and protein breakdown
 Theoretically, the anabolic state can also be
achieved through inhibition of muscle protein
breakdown. High-intensity training requires fuel
for energy.

The first line of energy comes from glycogen,

obtained from the food you eat, with the
secondary source coming from fatty acids.
The tertiary source or reserve tank is obtained
from amino acids
Building proteins
 Peptide bonds
 linking NH2 of one amino acid to
COOH of another
 C–N bond
 N terminus – C terminus

dehydration synthesis

peptide

bond
Protein structure & function
 Function depends on structure
 3-D structure
 twisted, folded, coiled into unique shape

pepsin

hemoglobin

collagen
Primary (1°) structure
 Order of amino acids in chain
 amino acid sequence determined by gene
(DNA)
 slight change in amino acid sequence can
affect protein’s structure & it’s function
 even just one amino acid change can make all
the difference!

lysozyme: enzyme in tears & mucus

that kills bacteria

Sickle cell anemia
Secondary (2°) structure
 “Local folding”
 folding along short
sections of polypeptide
 interaction between
adjacent amino acids
 H bonds between
backbones (O:H)
 -helix
 -pleated sheet
 Fibrous proteins – only have
secondary structure
 Keratin
 Silk
Secondary (2°) structure
 Tertiary (3°) structure
 “Whole molecule folding”
 created when the secondary structure
fold and form bonds to stabilize the
structure into a unique shape
 determined by interactions
between R groups
 Hydrophobic interactions
 anchored by
disulfide bridges
 Ionic Bonds between R groups
 Hydrogen bonds between backbones
 Van der Waals Force (velcro)
 Globular (spherical) proteins – have
tertiary structure
 enzymes
Quaternary (4°) structure
 two or more tertiary folded peptide subunits bonded
together to make a functional protein
Hemoglobin – 4 polypeptides
 Collagen – 3 polypeptides

collagen =

skin & tendons

hemoglobin
Protein structure (review)

R groups

hydrophobic interactions,
disulfide bridges, ionic bonds

3°
multiple

polypeptides

hydrophobic
1° interactions
aa sequence
peptide bonds

determined 2°

by DNA 4°
H bonds
Denature a protein
 Unfolding a protein/changes the shape
disrupt 3° structure
pH 
temperature
unravels or denatures protein
disrupts H bonds, ionic bonds &
disulfide bridges
destroys functionality
Eating Too Much Protein

Risk of heart disease

Risk of kidney stones

Risk of calcium loss from bones

Risk of colon cancer

Displacement of other nutrient-rich, disease preventing

foods
Eating Too Little Protein

PROTEIN-ENERGY MALNUTRITION (PEM)

 “PEM”: Invariably reflects combined deficiencies in…

 Protein: deficit in amino acids needed for cell structure,

function

 Energy: calories (or joules) derived from macronutrients:

protein, carbohydrate and fat

 Micronutrients: vitamin A, B-complex, iron, zinc,

calcium, others
 GROWTH DEFICIT IS CATALOGUED AS

• Clinical forms

– Marasmus

• Retarded growth with wasting of subcutaneous fat

• Shows a characteristic muscle wasting particularly

evident in the buttocks,

• pinched face and anxious

• Generally thought to be the result of cumulative,

usually slow, inadequate energy and protein
intake
– Kwashiorkor

• Growth failure with wasting of muscles

• preservation of subcutaneous fat

• pitting type edema: symmetric edema in the lower

limbs

• Hair is sparse

• Flaky paint rash on the buttocks, legs and arms

 – PEM

A.Mixed: Marasmus-Kwashiorkor (MK)

 Commonly coexist

 Need simple unified approach to clinical

management of both conditions

 clinically distinct entities

 Edema of kwashiorkor with wasting of marasmus

•MARASMUS
•Progressive wasting of the body and is associated with insufficient intake or malabsorption
of nutrients.
Characteristics of Marasmarus
• Occurs in children < 2 • Severe muscle
years of age wasting
• Severe deprivation • Low growth
(<60%), Low WAZ
• Develops slowly • No edema, no fatty
liver
• Severe weight loss • Anxiety, apathy
• “Old Man“ face, • Possible good
wrinkled appearance appetite
• Hair thin, dry; skin dry
KWASHIORKOR
Caused by lack of nutrients including protein in the diet

 1st to 3rd years of life

 Edema; enlarged fatty liver Growth: 60-80%

Apathy, misery, irritable
 Low protein, infections
Loss of appetite
Hair dry
 Rapid onset
Dermatosis (skin lesions)

 Some weight loss

 Some muscle wasting

Milder forms

• Wasting: Thinness using weight for height

(W/H)
• Stunting: Linear growth retardation using height
for age (H/A)
• Underweight

• A result of wasting and/or stunting

• Using weight for age (W/A)