PROTEIN

S
NAUREEN SHEHZADI
UNIVERSITY OF THE PUNJAB,
LAHORE
PROTEINS
Proteins are the
complex nitrogenous
compounds of high
molecular weight
formed naturally by
condensation of large
number of amino acids
through peptide bonds.
NUTRITIONAL VALUE
Nutritional value (Biological value; BV) of protein is determined
by amino acid composition;

High biological value proteins:

Protein that contains all essential amino acids in sufficient
proportions

Low biological value proteins:

Protein which is deficient (poor) in 1/more essential amino acids
SOURCES OF
PROTEINS
Animal proteins
Sources are;
• Meat
• Poultry
• Fish
• Eggs
• Milk
• Dairy products

Animal proteins are;

— Almost same proportion of each essential amino acid as human
protein
— Complete protein: high BV
Vegetable proteins
Sources include;
• Vegetables
• Legumes
• Plants
• Grains
• Nuts
• Seeds

Vegetable proteins are;

• Deficient in 1/more essential amino acids
• These are incomplete protein: low biological value
CLASSIFICATI
ON
Based on physicochemical properties
 PROTEINS (American
Society of Biological
Chemists)

SIMPLE CONJUGATE DERIVED

PROTEINS D PROTEINS PROTEINS

PRIMARY SECONDAR
DERIVED Y DERIVED
PROTEINS PROTEINS
 1- SIMPLE PROTEINS
Albumins
Globulins
Glutelins
Globular
Protamines
SIMPLE
PROTEINS Prolamins
(upon hydrolysis Histones
yield amino acids or
their derivatives Collagen
Fibrous Elastin
Keratin
1.1. Globular proteins
These are spherical or oval shape, soluble in water or other
solvents and digestible
Proteins Solubility Compositio Coagulation Examples
n
Albumins Water Deficient in By heat Egg
glycine albumin,
serum
albumin,
lactalbumin,
myosin
(muscles)

Globulins Dilute neutral Contain By heat and Serum

solutions of glycine precipitated globulin,
salts of alkali by half myosin
metals and saturation (muscles),
acids with ovoglobulin,
ammonium legumin
sulphate (legumes)
Protein Solubility Compositio Coagulation Example
n
Glutelins Dilute Glutelin
acids/alkalies (wheat),
Oryzenin
(rice)

Prolamins 70-80% Majorly Zein (corn),

alcohol proline and Hordein
deficient in (barley),
lysine Gliadin
(Wheat)
Protein Solubility Compositio Coagulation Example
n
Protamines Water, dilute Basic amino Not Salmine
ammonia, acids coagulated (Salmon
acids and (majorly by heat, sperm)
alkalies arginine) precipitate
other
proteins
from their
solutions
Histones Water, dilute Basic amino Not readily Globins
acids and acids coagulated (hemoglobin
alkalies by heat, ), histone
precipitate (thymus)
other
proteins
from their
solutions
1.2. Fibrous proteins
These are fibre like in shape, insoluble in water & resistance to
digestion.
Least soluble of all classes.
Constituents of exoskeletal structures…
Examples are keratin (hair, nail, horn, hoofs), elastin (connective
tissues), collagen (bone and cartilage), fibroin and sericin (silk)
2- CONJUGATED PROTEINS
Nucleoproteins

Glycoproteins
CONJUGATED
PROTEINS Mucoproteins
(simple proteins conjugated
to non-proteinous Phosphoproteins
substances; prosthetic
group, important Lipoproteins
constituents of enzymes)
Chymoproteins

Metalloproteins
Protein Composition Example
Nucleoproteins Simple proteins + Nucleohistones,
nucleic acid nucleoprotamins, oxidation-
reduction enzymes

Glycoproteins Simple proteins + Mucin (saliva), Albumin

carbohydrates (egg), Globulin (blood),
(glycosidic linkage) Casein (milk)

Mucoproteins Simple proteins + Gonadotropic hormones

mucopolysaccharides (follicle stimulating
hormone, interstitial cell
stimulating hormone, human
chorionic gonadotropin)
Protein Composition Example
Phosphoproteins Simple proteins + Casein (milk), Vitallin (egg
phosphate containing yolk)
substance (lecithin,
cephalin)
Lipoproteins Simple proteins + Lecithoprotein
lipid (lecithin,
cephalin, fatty acid)

Chromoproteins Simple proteins + Hemoglobin, catalase and

colored prosthetic cytochrome (heme),
group flavoproteins (riboflavin)

Metalloproteins Simple proteins + Hemoglobin and

metallic prosthetic cytochrome
group (Fe, Co, Mn,
Zn, Cu)
 3- DERIVED PROTEINS
Proteans
Primary derived
products
Metaproteins
DERIVED (denatured
PROTEINS proteins) Coagulated
(derived from simple proteins
and conjugated
proteins, include first Secondary Proteoses
step products of protein derived
degradation) products Peptones
(progressive
hydrolysis) Peptides
Protein Composition Example
Proteans Insoluble products formed as Myosan from
a result of hydrolysis of myosin
simple and conjugated
proteins by water, dilute
acids and enzymes
Metaproteins Products of acidic or alkaline Albuminates
degradation of simple
proteins insoluble in neutral
solutions

Coagulated Products of coagulation of Egg albumin,

proteins proteins by heat or alcohol cooked meat
(denatured proteins) proteins
Protein Composition
Proteoses Water soluble products, precipitated by
ammonium sulphate solution

Peptones Water soluble products, precipitated by

phosphotungstic acid

Peptides Hydrolytic cleavage to tetra, tri or di

peptides
CLASSIFICATI
ON
Based on their functions
 Structural proteins
Structural constituents of various cells and tissues;

1. Collagen is synthesized by fibroblasts and major extracellular

protein of connective tissues and bones.
2. Insoluble proteins with polar lipids constitute cell membrane.
3. Glycoproteins form cell coats and walls.
4. Elastin gives strength to the connective tissues.
5. Keratin is essential for healthy nails and hair.
 Storage proteins
These store certain species after conjugating with them e.g.

1. Ferritin stores iron in spleen

2. Oval albumin in eggs
3. Gliadin in wheat
4. Zein in corn
 Contractile proteins
Essential part of contractile and motile systems. Examples
include;

1. Myosin contractile protein of stationary filament of

myofibrils
2. Actin is contractile protein of moving filament of myofibrils
3. Dynenin is contractile protein of cilia and flagella
 Protective proteins
These play a very important role in circulatory system of
vertebrates. Examples include;

1. Antibodies in the blood defend the body against antigens

2. Fibrinogen is precursor of fibrin in blood clotting
3. Thrombin is also involved in blood coagulation
 Transport proteins
These proteins bind reversibly certain molecules and transport
them from one place to the other via blood stream. Examples
include;

1. Serum albumin binds free fatty acids and transport them to

other tissues or liver
2. Hemoglobin transports oxygen from lungs to various
respiration sites
 Enzymes
Enzymes catalyze biological reactions. Examples are;

1. Pepsin hydrolyses proteins in stomach

2. Alpha amylase degrades starch in mouth
3. Ribonuclease hydrolyses RNA
4. Cytochrome C transfers electron to oxygen in respiration
 Hormones
Hormones act as chemical messengers. Examples are;

1. Insulin which regulates glucose levels

2. Vasopressin regulates blood pressure
3. Adrenocorticotropic hormones
4. Growth hormones
 Toxins
Proteins secreted by microorganisms act as toxins (antigens).
PROPERTIES
PHYSICOCHEMICAL PROPERTIES
 CHEMICAL COMPOSITION
Chemical composition of various proteins is determined by
suitable quantitative methods. The approximate composition
includes;
• Carbon (47-50%)
• Hydrogen (6-7%)
• Oxygen (24-25%)
• Nitrogen (16-17%)
• Sulphur (0.2-0.3%)
PHYSICAL PROPERTIES
Physical state
Amorphous colloids
Taste
Tasteless, some are exceptionally bitter (Proteoses,
peptones amino acids and polypeptides)
Effect of heat
Irreversible coagulation upon heating (denaturation)
which changes the solubility, molecular shape, size, biological
activity and susceptibility to enzyme
Precipitation by salts
Coagulation by addition of different concentration of
suitable salts (salting out) e.g., ammonium sulphate. Most
proteins are precipitated by addition of acids e.g. trichloroacetic
acid, Perchloric acid, metaphosphoric acid etc. which occurs due
to acid insoluble salt formation.
Selective precipitation by solvents
Proteins precipitation may occur by adding suitable
amounts of alcohol. Alcohol lowers the dielectric constant of
aqueous system and hence reduces the solubility of proteins.
Dialysis
Proteins being colloidal in nature don't pass from
semipermeable membrane thus these can be freed from soluble
salts by cellophane membrane.
Ultracentrifugation
Different proteins sediment at different rates when their
solutions are spun at high speeds in an ultracentrifuge. Increase
in sedimentation is related to the increasing molecular weight of
protein. Method is useful in separating low molecular weight
proteins from higher.
Light scattering
Proteins scatter the light and this phenomenon is related
to their molecular size. This method is useful in determining the
molecular weights of proteins.
Proteins as charges ions
Zwitterion
Buffer action
Proteins present partly as their salt (zwitterion) and partly
as acidic form constitute buffer system i.e. upon addition of small
amounts of acids/base, prevent change in pH.
Optical activity
Proteins due to amino acids are optically active.
Viscosity
Depends on shape of molecule. Less symmetrical
molecule more solubility.
Electrophoresis
Proteins are positively charged in acidic solution and
negatively charged alkaline solution. Subject to the electric field,
anions move toward anode and cations towards cathode. Process
is called electrophoresis.
 CHEMICAL PROPERTIES
REACTION WITH NITROUS ACID
O

H2N CH C OH

CH3

OHNO

Nitrogen, Water + HO CH C OH

CH3
ACYLATION
O

H2N CH C OH

CH3

O
C
Ketene H2C

O O

C HN CH C OH

H3C CH3
SULFAHYDRAL CHAIN FORMATION

S
R
S S S
R-SH + +
S HS S

HS

S R
CLEAVAGE OF S-S GROUPS

S R'
+ 6 HCOOOH
R S

RSO3H + R'SO3H + 6HCOO- + 4H+

OXIDATION OF THIOL GROUP
HALOGENATION
REACTIONS WITH FORMALIN
CLASS ACTIVITY
Principle of protein identification tests
What is the difference between salting in and salting out?
What is the difference between full saturation and half saturation?
What is the principle of heat coagulation test and why dilute HCl is added to
the solution?