CHAPTER III PROTEINS

Functions of Proteins

 Proteins perform crucial roles in all biological processes.

 Catalytic:
- Most reactions in living organisms are catalyzed by proteins functioning as enzymes. Without
these catalysts, biological reactions would proceed much more slowly.
Key terms:
 Catalyst- speeds up the process of chemical reactions
 Enzymes- are proteins that help speed up metabolism, or the chemical reactions in our
bodies.

 Structural:
-In animal’s structural materials other than inorganic components of the skeleton are proteins,
such as collagen and keratin.
-gives the backbone of the proteins, and provides support, rigidity and elasticity
Key Terms:
 Collagen- is a hard, insoluble, and fibrous protein that makes up one-third of the protein
in the human body. In most collagens, the molecules are packed together to form long,
thin fibrils. These act as supporting structures and anchor cells to each other. They give
the skin strength and elasticity.
 Keratin- gives hydration/ reduce water loss in the skin

 Storage:
-Some proteins provide a way to store small molecules or ions, e.g., casein and ferritin.
Ket terms:
 Casein- provides the body with all of the amino acids necessary to help build muscle.
 Ferritin- a protein that stores iron inside your cells. You need iron to make healthy red
blood cells. Red blood cells carry oxygen from your lungs to the rest of your body.

 Protective:
-Antibodies are proteins that protect the body from disease by combining with and destroying
viruses, bacteria, and other foreign substances. Another protective function is blood clotting,
carried out by thrombin and fibrinogen.
Key Terms:
  Antibodies- is a protein produced by the body's immune system when it detects harmful
substances, called antigens. Examples of antigens include microorganisms (bacteria,
fungi, parasites, and viruses) and chemicals.
 Thrombin- is a coagulation protein in the bloodstream, which converts soluble
fibrinogen into insoluble strands of fibrin as well as catalyzing many other coagulation-
related reactions. When this substance travels in changes to embolus; A thrombus is a
blood clot that forms in a vein. An embolus is anything that moves through the blood
vessels until it reaches a vessel that is too small to let it pass.
 Fibrinogen- is the formation of fibrin that binds together platelets and some plasma
proteins in a hemostatic plug.
o One of the Blood Clothing Factors is the Blood Coagulation Cascade which is the
systematic flow of blood cloth

 Regulatory:
-Body processes regulated by proteins include insulin, growth hormone and thyrotropin.
Key Terms:
 Insulin- the net formation of protein is accelerated by insulin.
-produced in the pancreas β-cells create insulin while α-cells create glucagon
 Growth Hormone-stimulates protein anabolism in many tissues. This effect reflects
increased amino acid uptake, increased protein synthesis and decreased oxidation of
proteins.
 Thyrotropin- are key proteins in the control of thyroid function.

 Nerve impulse transmission:

- Some proteins act as receptors for small molecules that transmit impulses across the synapses
that separate nerve cells (e.g., Rhodopsin and acetylcholine).
Key Terms:
 Receptors- are proteins or glycoprotein that bind signaling molecules known as first
messengers, or ligands
 Rhodopsin- is the light receptor in rod photoreceptor cells of the retina that plays a
central role in phototransduction and rod photoreceptor cell health. It is the one gives
color perception
 Acetylcholine- is a type of chemical messenger, or neurotransmitter, that plays a vital
role in the central and peripheral nervous system. It is important for muscle control,
muscles relaxation, autonomic body functions, and in learning, memory, and attention.

 Movement:
-The proteins actin and myosin regulate the contraction of muscle fibers.
Key Terms:
 Actin- has a pivotal role in muscle contraction as well as in cell movements.
 Myosin- responsible for making the muscle relaxation.
  Transport:
-Some proteins bind small molecules or ions and transport them through the body. Serum
albumin is a blood protein that carries fatty acids between adipose tissue and other organs.
Hemoglobin carries oxygen from the lungs to other body tissues. Transferrin is a carrier of iron
in blood plasma.
Key Terms:
 Albumin- blood protein that carries fatty acids
 Adipose Tissue- provides protection, cushioning, and insulation
 Hemoglobin- carries oxygen from the lungs to other body tissues
 Transferrin- is a carrier of iron in blood plasma.

HOW PROTEINS ARE CREATED

Amides can be thought

of as forming from the
reaction of an amine and
a carboxylic acid:

In the same way, two

amino acids can
combine to form a
dipeptide, held together
by a peptide bond:

A third amino acid can

join the chain to form a
tripeptide:
Naming Proteins in a peptide chain

“In changing the name of amino acid residue on a peptide chain the suffix changes into -nyl, the
sequence starts from left to right where the last amino residue is left unchanged” example alanine
changes into alanyl

Chains of up to about 50 amino acids are polypeptides, and chains of more than 50 amino acids are
proteins. Amino acids in peptide chains are called amino acid residues. The residue with a free amino
group is called the N-terminal residue, and is written on the left end of the chain. The residue with a free
carboxylate group is called the C-terminal residue, and is written on the right end of the chain. Peptides
are named by starting at the N-terminal end and listing the amino acid residues from left to right.

PROTEIN STRUCTURES

Primary Structure

The primary structure of a

protein is the linear sequence
of the side chains that are
connected to the protein
backbone:
Each protein has a unique sequence of amino acid residues that cause it to fold into a distinctive
shape that allows the protein to function properly.

Secondary Structure

Hydrogen bonding causes protein chains to fold

and
In align to myosin
a-keratin, produce(muscles),
orderly patterns called
secondary(skin),
epidermin structures. The a-helix
and fibrin is a single
(blood clots),
two or more helices coil together coiled helical
protein chain twisted to resemble a
spring.
(supracoiling) to form cables. These
cables make up bundles of fibers that
strengthen tissues in which they are
found.

Another secondary structure is the b-

pleated sheet, in which several protein
chains lie side by side, held by hydrogen
bonds between adjacent chains.
Quaternary Structure

When two or more polypeptide chains are held

together by disulfide bridges, salt bridges,
hydrogen bond, or hydrophobic interactions, it
forms a larger protein complex.
SulfurEach
Ion of the
polypeptide subunits has its own primary,
secondary, and tertiary structure. The arrangement
of the subunits to form a larger protein is the
quaternary structure of the protein.

Neutralization

“salting out”

Hemoglobin
CLASSIFICATION OF PROTEINS

1. Globular: Polypeptide chain(s) of these proteins are folded into compact globular (Spherical)
shape. Examples: Hemoglobin, myoglobin, albumin, lysozyme, chymotrypsin.
Key terms:
 Hemoglobin- carries oxygen from the lungs to other body tissues
 Myoglobin- facilitates oxygen diffusion.
 Albumin- blood protein that carries fatty acids
 Lysosome- known as terminal catabolic stations that rid cells of waste products and
scavenge metabolic building blocks that sustain essential biosynthetic reactions during
starvation.
 Chymotrypsin- is used in the small intestine to break down proteins into individual
amino acids

2. Fibrous: Polypeptide chains are extended along one axis. Examples: α-keratin, β- keratin,
collagen and elastin.
Key Terms:
 α-keratin- are structural components of the outer layer of human skin and are integral to
hair, nails, claws, feathers, beaks, scales, and hooves. Keratins provide strength to
tissues, such as the tongue, and over 50 different keratins are encoded in the human
genome.
 β- keratin- do much more rigidity to reptilian skin than alpha-keratins alone due to
mammalian skin. β-keratins are impregnated into the stratum corneum of the reptilian
skin, providing waterproofing and the prevention of desiccation.
 Collagen- is a hard, insoluble, and fibrous protein that makes up one-third of the protein
in the human body. In most collagens, the molecules are packed together to form long,
thin fibrils. These act as supporting structures and anchor cells to each other. They give
the skin strength and elasticity.
 Elastin- allow tissues in your body to stretch out and shrink back. Your arteries are tube-
shaped blood vessels that carry blood from your heart through your body. Elastin gives
your arteries stretchy characteristics that make it easier for your heart to pump blood.
Protein Folding
Proteins are too large to pass through cell membranes, and are contained within the cells where
they were formed unless the cell is damaged by disease or trauma. Persistent large amounts of protein
in the urine are indicative or damaged nephrons. Myocardial Infarction can also be confirmed by the
presence of certain proteins in the blood that are normally confined to cells in heart tissue.

The amino acids in the protein all fold into a complex 3D shape that actually makes it all functional.
Hemoglobin when folded has a perfect spot to bind an oxygen molecule, and when it reaches its
destination it also perfectly changes shape to release that oxygen molecule.

Key terms:

 Nephrons- is the basic structural and functional unit of the kidney

 Myocardial Infarction- happens when one or more areas of the heart muscle don't get enough
oxygen. This happens when blood flow to the heart muscle is blocked.
 Proteinuria- is a high level of protein in your urine (pee). This condition can be a sign of kidney
damage. Proteins have many important functions, including: Building muscles and bones.
Regulating the amount of fluid in your blood.

Proteins are maintained in their native state (their natural 3D conformation) by stable secondary and
tertiary structures, and by aggregation of subunits into quaternary structures. Denaturation is caused
when the folded native structures break down because of extreme temperature or pH values, which
disrupt the stabilizing structures. The structure becomes random and disorganized.

Most proteins are biologically active only over a temperature range of 0C to 40C. Heat is often used to
kill microorganisms and deactivate their toxins. The protein toxin from Clostridium botulinum,
diphtheria and tetanus is inactivated by being heated to 100oC for a few minutes.

Heat denaturation is used to prepare vaccines against some diseases. The denatured toxin can no longer
cause the disease, but it can stimulate the body to produce substances that induce immunity.

Heavy-metal poisoning is often treated with large doses of raw egg white and milk; the proteins in the
egg and milk bind to the metal ions this bonding is called chelation, forming a precipitate, which is either
vomited out or pumped out.

There are 35 metals that are of concern for us because of residential or occupational exposure, out of
which 23 are heavy metals: antimony, arsenic, bismuth, cadmium, cerium, chromium, cobalt, copper,
gallium, gold, iron, lead, manganese, mercury, nickel, platinum, silver, tellurium, thallium, tin,
uranium, vanadium, and zinc.
Nitrogen-balance
Determines the protein requirements of the body throughout the life cycle and to assign value to
the protein quality of foods to determine their biologic value. Nitrogen Balance being the amount of
nitrogen being absorbed vs the amount being excreted. Nitrogen excreted from the body may be
endogenous, metabolic (from intestinal cells), or exogenous nitrogen. Nitrogen in feces may be
metabolic and exogenous while in urine may be endogenous and exogenous.

 Nitrogen equilibrium or zero nitrogen balance

-occurs if the amount of nitrogen consumed in foods equals the amount excreted. Because
adults are no longer growing, the nitrogen that enters the body is not needed to build new
tissue but is used simply to maintain the body.

 Positive nitrogen balance

-occurs when more nitrogen is retained in the body than excreted. The nitrogen is used to form
new cells for growth or healing, so it occurs in individuals recovering from injury, growing
children and pregnant women who require additional protein for fetal growth.

 Negative nitrogen balance

-happens when more nitrogen is excreted from the body than is retained from diet. This occurs
when there is a breakdown of proteins in muscles and organs due to aging, physical illness,
extreme stress, starvation, surgery, or eating disorders.
Complex Proteins
Immunoglobulins (IG) are globulins
produced as body’s immune or defense against
infection. Infection is the invasion of body by
virus or microorganisms or foreign molecules.
They are produced by B-lymphocytes, bone
marrow and spleen in response to infection.
Entry of foreign molecule into body triggers the
synthesis of specific globulin, which selectively
combines with foreign molecule and lead to its
inactivation. The foreign molecule is called as
antigen whereas globulin produced against it is
called as antibody.

Key Terms:

 Immunoglobulins- also known as antibodies, are glycoprotein molecules produced by plasma

cells (white blood cells)
 Infection- is the invasion of body by virus or microorganisms or foreign molecules
 Antigen- Any substance that causes the body to make an immune response against that
substance. Antigens include toxins, chemicals, bacteria, viruses, or other substances that come
from outside the body.
 Antibody- A protein made by plasma cells (a type of white blood cell) in response to an antigen
(a substance that causes the body to make a specific immune response)

Albumin
Liver produces about 12 grams of albumin per day.
Albumin accounts for 75% of the osmotic pressure (25 mm Hg) in
blood and responsible for maintenance of blood volume. It has a
major role in the regulation of fluid distribution. One gram of
albumin holds 18 ml of fluid in the blood stream. Decrease in
albumin level leads to accumulation of fluid which results in
edema. It transports fatty acids from adipose tissue to liver.

Key Terms:

 Albumin- a simple form of protein that is soluble in water and coagulable by heat, such as that
found in egg white, milk, and (in particular) blood serum.
Clinical Significance of Proteins
Disorders associated with high or low serum concentrations of specific are :

 Transferrin and ferritin are used to assess iron status

 Ceruloplasmin reflects copper transport and storage
 Cardiac troponins reveal myocardial damage
 Tumor markers such as prostate-specific antigen (PSA)
 Alpha fetoprotein (AFP)
 carbohydrate antigen (CA) markers
 carcinoembryonic antigen (CEA), are used to detect, and monitor treatment of cancer
 fibrinogen and coagulation factors are used to assess hemostatic function
 Chemical Properties with Physiological Activity

Charge properties: Charge of a protein depends

on the surroundings like amino acids. So, by
changing the pH of surroundings the charge of
protein can be altered. This property is used for
separation of proteins. 

Isoelectric point: At the isoelectric point, its

net charge is zero because the number of positive
charges is equal to number of negative charges.
So, proteins are insoluble or have minimum
solubility at isoelectric point. This property is used
for the isolation of casein from milk. 

Proteins act as buffers: Since proteins are

amphoteric substances, they act as buffers.
Hemoglobin (Hb) of erythrocytes and plasma
proteins are important buffers.