PROTEINS

Next to water, proteins are the most abundant substances in nearly all cells — they account for about
15% of a cell’s overall mass (Section 18.1) and for almost half of a cell’s dry mass. All proteins contain
the elements carbon, hydrogen, oxygen, and nitrogen; most also contain sulfur.

The average nitrogen content of proteins is 15.4% by mass. Other elements, such as phosphorus and
iron, are essential constituents of certain specialized proteins. Casein, the main protein of milk,
contains phosphorus, an element very important in the diet of infants and children. Hemoglobin, the
oxygen-transporting protein of blood, contains iron. A protein is a naturally occurring, unbranched
polymer in which the monomer units are amino acids.

AMINO ACIDS: THE BUILDING BLOCKS FOR PROTEIN

An amino acid is an organic compound that contains both an amino (! NH2) group and a carboxyl (!
COOH) group. The amino acids found in proteins are always a-amino acids. An -amino acid is an amino
acid in which the amino group and the carboxyl group are attached to the -carbon atom. The general
structural formula for an -amino acid is a-Carbon atom Carboxyl group Side chain H H2N O R A O COOH
A Amino C group The R group present in an a-amino acid is called the amino acid side chain.

➢ A standard amino acid is one of the 20 a-amino acids normally found in proteins. The structures
of the 20 standard amino acids are given
➢ amino acids are grouped according to side-chain polarity.
there are four categories: (1) nonpolar amino acids, (2) polar neutral amino acids, (3) polar
acidic amino acids, and (4) polar basic amino acids.

I. A nonpolar amino acid is an amino acid that contains one amino group, one carboxyl group, and
a nonpolar side chain.

The nonpolar amino acid proline has a structural feature not found in any other standard
amino acid.

There are nine nonpolar amino acids. Tryptophan is a borderline member of this group
because water can weakly interact through hydrogen bonding with the NH ring location on
tryptophan’s side-chain ring structure.

II. A polar neutral amino acid is an amino acid that contains one amino group, one carboxyl group,
and a side chain that is polar but neutral.
In solution at physiological pH, the side chain of a polar neutral amino acid is neither acidic
nor basic. There are six polar neutral amino acids. These amino acids are more soluble in water
than the nonpolar amino acids as, in each case, the R group present can hydrogen bond to water

III. A polar acidic amino acid is an amino acid that contains one amino group and two carboxyl
groups, the second carboxyl group being part of the side chain.
 In solution at physiological pH, the side chain of a polar acidic amino acid bears a negative
charge; the side-chain carboxyl group has lost its acidic hydrogen atom. There are two polar
acidic amino acids: aspartic acid and glutamic acid. These non-amino acid components, which
may be organic or inorganic, are called prosthetic groups. A prosthetic group is a non-amino acid
group present in a conjugated protein.

IV. A polar basic amino acid is an amino acid that contains two amino groups and one carboxyl
group, the second amino group being part of the side chain. In solution at physiological pH, the
side chain of a polar basic amino acid bears a positive charge; the nitrogen atom of the amino
group has accepted a proton (basic behavior; Section 17.6). There are three polar basic amino
acids: lysine, arginine, and histidine.

The Essential Amino Acids

An essential amino acid is an amino acid needed in the human body that must be obtained from
dietary sources because it cannot be synthesized within the body from other substances in
adequate amounts.
The Essential Amino Acids for Humans
arginine*, methionine, histidine, phenylalanine, isoleucine, threonine, leucine, tryptophan,
lysine, valine
*Arginine is required for growth in children but is not required by adults.

A complete dietary protein is a protein that contains all the essential amino acids in
approximately the same relative amounts in which the human body needs them.
- A complete dietary protein may or may not contain all the nonessential amino acids.
- Most animal proteins, including casein from milk and proteins found in meat, fish, and eggs,
are complete proteins, although gelatin is an exception (it lacks tryptophan). Proteins from
plants (vegetables, grains, and legumes) have quite diverse amino acid patterns and some
tend to be limited in one or more essential amino acids.
- Some plant proteins (for example, corn protein) are far from complete. Others (for example,
soy protein) are complete.
- The following table lists the essential amino acid deficiencies associated with selected
vegetables and grains.

FOOD SOURCE AMINO ACID DEFIECIENCY

. soy none
wheat, rice, oats lysine
corn lysine, tryptophan
beans methionine, tryptophan
peas methionine
almonds, walnuts lysine, tryptophan
 CHIRALITY AND AMINO ACIDS

Four different groups are attached to the a-carbon atom in all of the standard amino acids
except glycine, where the R group is a hydrogen atom.

- Glycine, the simplest of the standard amino acids, is achiral. All of the other standard amino
acids are chiral.
- Two of the 19 chiral standard amino acids, isoleucine and threonine, possess two chiral
centers. With two chiral centers present, four stereoisomers are possible for these amino
acids. However, only one of the L isomers is found in proteins.

ACID-BASE PROPERTIES OF AMINO ACIDS

In pure form, amino acids are white crystalline solids with relatively high decomposition
points. (Most amino acids decompose before they melt.) Also, most amino acids are not
very soluble in water because of strong intermolecular forces within their crystal structure.
Such properties are those often exhibited by compounds in which charged species are
present. Studies of amino acids confirm that they are charged species both in the solid
state and in solution.

- we learned that in neutral solution, carboxyl groups have a tendency to lose protons (H),
producing a negatively charged species:
- we learned that in neutral solution, amino groups have a tendency to accept protons (H),
producing a positively charged species:

ZWITTERION
- from the German term meaning “double ion.” A zwitterion is a molecule that has a positive
charge on one atom and a negative charge on another atom, but which has no net charge.
- Note that the net charge on a zwitterion is zero even though parts of the molecule carry
charges.
- Zwitterion structure changes when the pH of a solution containing an amino acid is
changed from neutral either to acidic (low pH) by adding an acid such as HCl or to basic
(high pH) by adding a base such as NaOH. In an acidic solution, the zwitterion accepts a
proton (-) to form a positively charged io.
- Strong intermolecular forces between the positive and negative centers of zwitterions are
the cause of the high melting points of amino acids.
- the structures of amino acids will be drawn in their zwitterion form unless information given
about the pH of the solution indicates otherwise.
- In basic solution, the -NH3 of the zwitterion loses a proton, and a negatively charged species
is formed.
- The ability of amino acids to react with both H3O and OH ions means that amino acid
solutions can function as buffers. The same is true for proteins, which are amino acid
polymers. The buffering action of proteins present in blood is a major function of such
proteins.
- Guidelines for amino acid form as a function of solution pH follow. Low pH: All acid groups
are protonated (!COOH). All amino groups are protonated (! N H3). High pH: All acid groups
are deprotonated (!COO ). All amino groups are
deprotonated (!NH2). Neutral pH: All acid groups are deprotonated (!COO
). All amino groups are protonated (!N H3).
- The term protonated denotes gain of a Hion, and the term deprotonated denotes loss of a
Hion

Isoelectric Points and Electrophoresis

- The amounts of the various forms of an amino acid — zwitterion, negative ion(s), and
positive ion(s) — that are present in an aqueous solution of the amino acid vary with
solution pH. There is no pH at which ionic amino acid forms are absent, but there is a pH at
which there is an equal number of positive and negative charges present, which produces a
“no net charge” situation.
- The “no net charge” pH value for an amino acid solution is called its isoelectric point. An
isoelectric point is the pH at which an amino acid solution has no net charge because an
equal number of positive and negative charges are present
- Every amino acid has a different isoelectric point. Fifteen of the 20 amino acids, those with
nonpolar or polar neutral side chains. The isoelectric point of an amino acid is measured by
observing its behavior in an electric field.
- In an electric field, a charged molecule is attracted to (migrates toward) the electrode of
opposite charge. At a high pH, an amino acid has a net negative charge and migrates toward
the positive electrode. At a low pH, the opposite is true; with a net positive charge, the
amino acid migrates toward the negative electrode. At the isoelectric point, migration does
not occur because the zwitterions present have no net charge, have isoelectric points in the
range of 4.8–6.3. The three basic amino acids have higher isoelectric points and the two
acidic amino acids have lower ones.
- Electrophoresis is the process of separating charged molecules on the basis of their
migration toward charged electrodes associated with an electric field.
- When a current is applied, Phe does not move (it has no net charge); Lys, because of its
positive charge, migrates toward the negative electrode; and Glu, with a negative charge,
moves toward the positive electrode. Proteins, which are amino acid polymers, also have
isoelectric points and also can be separated via electrophoresis techniques.
 CYSTEINE: A CHEMICALLY UNIQUE AMINO ACID

- Cysteine is the only standard amino acid that has a side chain that contains a sulfhydryl
group.
- The presence of this sulfhydryl group imparts to cysteine a chemical property that is unique
among the standard amino acids.
- Cysteine, in the presence of mild oxidizing agents, readily dimerizes, that is, reacts with
another cysteine molecule to form a cystine molecule.
- A dimer is a molecule that is made up of two like subunits.) In cystine, the two cysteine
residues are linked via a covalent disulfide bond.
- Cystine contains two cysteine residues linked by a disulfide bond.
- The covalent disulfide bond of cystine is readily broken, using reducing agents, to
regenerate two cysteine molecules.

PEPTIDES
- amino acids can bond together to produce an unbranched chain of amino acids, each joined
to the next by a peptide bond.
- A compound containing two amino acids is specifically called a dipeptide;
- three amino acids joined together in a chain constitute a tripeptide;
- The name oligopeptide is loosely used to refer to peptides with 10 to 20 amino acid
residues
- A polypeptide is a long unbranched chain of amino acids, each joined to the next by a
peptide bond

Nature of the Peptide Bond

- The bonds that link amino acids together in a peptide chain are called peptide bonds.
- The nature of the peptide bond becomes apparent by reconsidering a chemical reaction
previously encountered.
- Amide bond formation is an example of a condensation reaction.
- A peptide chain has directionality because its two ends are different.
- A peptide bond is a covalent bond between the carboxyl group of one amino acid and the
amino group of another amino acid.
- An amino acid residue is the portion of an amino acid structure that remains, after the
release of H2O, when an amino acid participates in peptide bond formation as it becomes
part of a peptide chain.
- The R group side chains are considered substituents on the backbone rather than part of the
backbone.
- Thus, structurally, a peptide has a regularly repeating part (the backbone) and a variable
part (the sequence of R groups). It is the variable R group sequence that distinguishes one
peptide from another.

Isomeric Peptides

- Peptides that contain the same amino acids but in different order are different molecules
(constitutional isomers) with different properties.
- Amino acid sequence in a peptide has biochemical importance. Isomeric peptides give
different biochemical responses; that is, they have different biochemical specificities.
- The number of isomeric peptides possible increases rapidly as the length of the peptide
chain increases.

BICHEMICALLY IMPORTANT SMALL PEPTIDES

- Many relatively small peptides have been shown to be biochemically active. Functions for
them include hormonal action, neurotransmission, and antioxidant activity.

SMALL PEPTIDE HORMONES

- The two best-known peptide hormones, both produced by the pituitary gland, are oxytocin
and vasopressin.
- Oxytocin plays a role in stimulating the flow of milk in a nursing mother. The baby’s suckling
action sends nerve signals to the mother’s brain, triggering the release of oxytocin, via the
blood, to the mammary glands. The oxytocin causes muscle contraction in the mammary
gland, forcing out milk. As suckling continues, more oxytocin is released and more milk is
available for the baby.
- Oxytocin regulates uterine contractions and lactation. Vasopressin regulates the excretion
of water by the kidneys; it also affects blood pressure.

Small Peptide Neurotransmitters

- Enkephalins are pentapeptide neurotransmitters produced by the brain itself that bind at
receptor sites in the brain to reduce pain.
- The two best-known enkephalins are Metenkephalin and Leu-enkephalin, whose structures
are
Met-enkephalin: Tyr–Gly–Gly–Phe–Met
Leu-enkephalin: Tyr–Gly–Gly–Phe–Leu
- The two enkephalins differ structurally only in the amino acid at the end of the chain.
- The pain-reducing effects of enkephalin action play a role in the “high” reported by long-
distance runners, in the competitive athlete’s managing to finish the game despite being
injured, and in the pain-relieving effects of acupuncture.
- The action of the prescription painkillers morphine and codeine is based on their binding at
the same receptor sites in the brain as the naturally occurring enkephalins.

Small Peptide Antioxidants

- The tripeptide glutathione (Glu–Cys–Gly) is present in significant concentrations in most
cells and is of considerable physiological importance as a regulator of oxidation–reduction
reactions. Specifically, glutathione functions as an antioxidant (Section 14.13), protecting
cellular contents from oxidizing agents such as peroxides and superoxides (highly reactive
forms of oxygen often generated within the cell in response to bacterial invasion).

GENERAL STRUCTURAL CHARACTERISTICES OF PROTEINS

- Proteins are the second type of biochemical polymer we have encountered; the other was
polysaccharides. Protein monomers are amino acids, whereas polysaccharide monomers are
monosaccharides
- A protein is a peptide in which at least 40 amino acid residues are present.
- proteins are classified as monomeric or multimeric.

➢ A monomeric protein is a protein in which only one peptide chain is present. Large
proteins, those with many amino acid residues, usually are multimeric.
➢ A multimeric protein is a protein in which more than one peptide chain is present.
The peptide chains present in multimeric proteins are called protein subunits.
➢
- Proteins, on the basis of chemical composition, are classified as simple or complex.
• A simple protein is a protein in which only amino acid residues are present. More
than one protein subunit may be present in a simple protein, but all subunits
contain only amino acids.
• A conjugated protein is a protein that has one or more nonamino acid entities
present in its structure in addition to one or more peptide chains.
• These non-amino acid components, which may be organic or inorganic, are called
prosthetic groups. A prosthetic group is a non-amino acid group present in a
conjugated protein.
• Conjugated proteins may be further classified according to the nature of the
prosthetic group(s) present.
- Lipoproteins contain lipid prosthetic groups,
- glycoproteins contain carbohydrate groups,
- metalloproteins contain specific metal
- prosthetic groups have important roles in the biochemical functions for conjugated
proteins.
 PRIMARY STRUCTURE OF PROTEIN
➢ Primary protein structure is the order in which amino acids are linked together in a protein.
- Primary protein structure always involves more than just the numbers and kinds of amino
acids present; it also involves the order of attachment of the amino acids to each other
through peptide bonds.
- Insulin, the hormone that regulates blood-glucose levels, was the first protein for which
primary structure was determined; the “sequencing” of its 51 amino acids was completed in
1953, after 8 years of work by the British biochemist Frederick Sanger.
- The primary structure of a specific protein is always the same regardless of where the
protein is found within an organism.
- The actual shape of the protein is determined by secondary and tertiary levels of protein
structure, levels yet to be discussed.
- The primary structure of a protein is the sequence of amino acids in a protein chain — that
is, the order in which the amino acids are connected to each other
- Proteins are formed from proper sequences of the 20 standard amino acids.

Substitutes for Human Insulin

- In humans, an insufficient production of insulin results in the disease diabetes mellitus

- because of the limited availability of human insulin, most insulin used by diabetics was
obtained from the pancreases of slaughter-house animals.

SECONDARY STRUCTURE OF PROTEIN

- Secondary protein structure is the arrangement in space adopted by the backbone portion
of a protein
- The two most common types of secondary structure are the alpha helix (a helix) and the
beta pleated sheet (B pleated sheet).
- The type of interaction responsible for both of these types of secondary structure is
hydrogen bonding between a carbonyl oxygen atom of a peptide linkage and the hydrogen
atom of an amino group of another peptide linkage farther along the backbone.
- Information about the geometry associated with these peptide linkages is helpful in
understanding how hydrogen bonding interactions occur between peptide linkages of a
protein backbone.
 ➢ An active area of protein research at present involves learning more about the biochemical
functions for the unstructured portions of proteins. A growing number of researchers now
believe that some “unstructure” is essential to the functioning of many proteins. It confers
➢ flexibility to proteins, thereby allowing them to interact with several different substances, an
important mechanism for rapid response to changing cellular conditions.
➢ The act of binding to another protein does bring added structure to the unstructured portion of
the protein, but the added structure is lost when the binding interaction ceases
➢ The term unstructured used in describing portions of a protein structure is somewhat of a
misnomer, because all molecules of a given protein exhibit identical unstructured segments.

The Alpha Helix

- An alpha helix structure is a protein secondary structure in which a single protein chain
adopts a shape that resembles a coiled spring (helix), with the coil configuration
maintained by hydrogen bonds

The Beta Pleated Sheet

- A beta pleated sheet structure is a protein secondary structure in which two fully extended
protein chain segments in the same or different molecules are held together by hydrogen
bonds.
- The term pleated sheet arises from the repeated zigzag pattern in the structure

TERTIARY STRUCTURE OF PROTEIN

- Tertiary protein structure is the overall three-dimensional shape of a protein that results
from the interactions between amino acid side chains (R groups) that are widely separated
from each other within a peptide chain
- A good analogy for the relationships among the primary, secondary, and tertiary structures
of a protein is that of a telephone cord
- The coiling of the cord into a helical arrangement gives the secondary structure. The
supercoiling arrangement the cord adopts after you hang up the receiver is the tertiary
structure.

Interactions Responsible for Tertiary Structure

(1) covalent disulfide bonds - the strongest of the tertiary-structure interactions

- may involve two cysteine units in the same peptide chain; or two cysteine units in different
chains

(2) electrostatic attractions- also called salt bridges, always involve the interaction between an
acidic side chain (R group) and a basic side chain (R group).
 (3) hydrogen bonds- can occur between amino acids with polar R groups.

(4) Hydrophobic interactions- result when two nonpolar side chains are close to each other.

QUARTERNARY STRUCTURE OF PROTEIN

- Quaternary structure is the highest level of protein organization. It is found only in

multmeric protein.
- Quaternary protein structure is the organization among the various peptide chains in a
multimeric protein.

PROTEIN CLASSIFICATION BASED ON SHAPE

1. fibrous protein is a protein whose molecules have an elongated shape with one dimension
much longer than the others. Fibrous proteins tend to have simple, regular, linear structures.
2. A globular protein is a protein whose molecules have peptide chains that are folded into
spherical or globular shapes. Generally, globular proteins are water-soluble substances.
3. membrane protein is a protein that is found associated with a membrane system of a cell.
Membrane protein structure is somewhat opposite that of globular proteins, with most of the
hydrophobic amino acid side chains oriented outward. Thus, such proteins tend to be water
insoluble and they usually have fewer hydrophobic amino acids than globular proteins.

Keratin

- The fibrous protein keratin is particularly abundant in nature, where it is found in protective
coatings for organisms.
- It is the major protein constituent of hair, feathers, wool, fingernails and toenails, claws,
scales, horns, turtle shells, quills, and hooves.
- Natural silk (silkworm silk) and spider silk (spider webs) are made of fibroin, a fibrous
protein that exists mainly in a beta pleated sheet form. The great strength and toughness of
silk fibers, which exceed those of many synthetic fibers, is related to the close stacking of
the beta sheets.
 - Protofilaments then coil together in groups of four to form microfilaments , which become
the “core” unit in the structure of the keratin of hair
- Particularly important are intercoil disulfide bridges that form between cysteine residues.
- Introduction of disulfide bridges within the several levels of coiling structure determines
the “hardness” of an keratin.

Collagen

- the most abundant of all proteins in humans

- a major structural material in tendons, ligaments, blood vessels, and skin
- it is also the organic component of bones and teeth.
- Cross-linking between helices gives the fibrils extra strength.
- The greater the number of cross links, the more rigid the fibril is

Hemoglobin

- The globular protein hemoglobin transports oxygen from the lungs to tissue.
- It is a tetramer (four peptide chains) with each subunit also containing a heme group, the
entity that binds oxygen.
- With four heme groups present, a hemoglobin molecule can transport four oxygen
molecules at the same time.
- fetal hemoglobin, this hemoglobin has a greater affinity for oxygen than the mother’s
hemoglobin. This ensures a steady flow of oxygen to the fetus

Myoglobin

- The globular protein myoglobin functions as an oxygen storage molecule in muscles.

- Myoglobin is a monomer
- myoglobin consists of a single peptide chain and a heme unit
- function of myoglobin is oxygen storage.

Protein Structure and the Color of Meat

- The major proteins present in such muscle tissue are myosin and actin,
- Contraction is temporarily maintained through interactions between these two types of
proteins.
- The amount of myoglobin present in a muscle is determined by how the muscle is used
- The amount of myoglobin present in muscle tissue is a major determiner of the color of the
muscle tissue
- Myoglobin molecules have a red color when oxygenated and a purple color when
deoxygenated
- The different colors of meat reflect the concentration of myoglobin in the muscle tissue
 PROTEIN CLASSIFICATION BASED ON FUNCTION

- Proteins play crucial roles in almost all biochemical processes. The diversity of functions
exhibited by proteins far exceeds that of other major types of biochemical molecules.
- The functional versatility of proteins stems from (1) their ability to bind small molecules
specifically and strongly to themselves, (2) their ability to bind other proteins, often other
like proteins, to form fiber-like structures, and (3) their ability to bind to, and often become
integrated into, cell membranes.

1. Catalytic proteins.
- Proteins are probably best known for their role as catalysts. Proteins with the role of
biochemical catalyst are called enzymes. Enzymes participate in almost all of the metabolic
reactions that occur in cells.

2. Defense proteins.
- These proteins, also called immunoglobulins or antibodies , are central to the functioning
of the body’s immune system. They bind to foreign substances, such as bacteria and
viruses, to help combat invasion of the body by foreign particles

Protein hydrolysis;
When a protein or smaller peptide solution of strong acid and base is heated, the peptide bonds
of the amino acid chain are hydrolyzed and free amino acid are produced. The hydrolysis reaction is the
reverse of the formation reaction for a peptide. Amine and hydrolytic acid functional group are
regenerated.
In complete hydrolysis all peptide bonds are broken freeing up all of the constituent amino acids;
In partial protein hydrolysis some, but not all , of the peptide bonds are broken producing a
product mixture that contains both amino acids and small peptides.

Protein Denaturation: is the partial or complete disorganization of protein’s characteristic three

dimensional shape as a result of disruption of its secondary, tertiary and quarternary structure of
protein

2 Kinds of Denaturation

a. Reversible denaturation - the condition for denaturation is mild , the protein can be restored
to its original conformation by carefully reversing the condition that cause denaturation
Example; curling of hair
b. Irrevesible denaturation - the condition for denaturation is drastic ; the protein will or
precipitate from solution coagulate

Reagents or Condition that cause Denaturation;

Denaturing Agent Mode of Action

 1.Heat Disrupt hydrogen bond by making molecules to vibrate too
violently; produces coagulation as in frying of an eff
2. microwave radiation Causes violent vibration of molecules that disrupt hydrogen
bonds
3. ultraviolet radiation Operates very similarly to the action of heat ; example
sunburning
4. violent whipping or shaking Causes molecules in globular shapes to extend to longer
length, which then entangles ; Example beating egg white
into meringue.
5. detergent Affects R-group interaction
6. Organic solvents Ex.ethanol, Interfere with R- group interactions because these solvents
acetone, 2-propanol also can form hydrogen bonds; quickly denatures protein in
bacteria ; killing them Ex; the disinfectant action of 70%
ethanol.
7. strong acids and bases Disrupt hydrogen bonds and salt bridges; prolonged action
leads to actual hydrolysis of peptide bonds
8. Salts of heavy metals Ex; salts of Metal ions combine with – SH groups and form poisonous
(Hg2+, Ag+, Pb2+ )
9. oxidizing and reducing agent Denature protein irreversibly by disrupting the disulfide
bonds. Reducing agent reduces linkages to produce - SH
group
10. Alkaloidal reagents Denature protein irreversibly by disrupting the disulfide
bond

11. pH Changes in Ph can disrupt hydrogen bond and salt bridges

causing irreversible denaturation

Classification of Protein Based on Shape

1. Globular protein – is a protein whose molecules have peptide bonds that are folded into
spherical or globular shapes.. Consists of polypeptide folded into shape of ”‘balls”. They have a
length to with ration of less than 10. Globular proteins are soluble in water and form colloidal
dispersion and have an active function; Examples; hemoglobin, albumin, globulins

2. Fibrous proteins – consists of parallel polypeptide chains are coiled and stretch out. Length to
with ratio is greater than 10. Fibrous proteins are insoluble in water. They include collagen,
fibrin amd myosin

Common Fibrous and Globular Proteins

Name Occurrence and Function

 Fibrous Protein
Keratin Found in wools, feathers, hooves, silk and fingernails
Collagen Found in tendons, bones, and other connective tissues
Elastin Found in blood vessels and ligaments
Myosin Found in muscle tissue
fibrin Found in blood clots
Globular proteins
Insulin Regulatory hormone for glucose metabolism
Myoglobin Involved in oxygen storage in muscles
Hemoglobin Involved in oxygen transport in blood
Transferrin Involved in iron transport in blood
immunoglobulin In volved in immune system responses

Alpha -keratin – abundant in nature, where it is found in protective coatings for organism. It is the
major component of hair feathers, wool, fingernails, scales, and hooves

Collagen, most abundant of all proteins in human, It is also the major structural material in tendons,
ligaments, blood vessel and skin, It is also the organic component of bones and teeth.

Hemoglobin – globular proteins that transport oxygen from lungs to tissue

Myoglobin – is a globular protein that function as an oxygen storage molecule in muscles. Oxygen
stored in myoglobin molecules serves as a source of working muscles when their demand for oxygen
exceed that which can be supplied by hemoglobin

Glycoprotein – is a protein that contains carbohydrates or carbohydrate derivative in addition to amino

acids.

Immunoglobulin are among the most important and interesting of the soluble proteins in human body
Immunoglobulin is a glycoprotein produced by an organism as a protective response to the invasion of
microorganism s or foreign molecules.

Immunoglobulin – serves as antibodies to combat invasion of the body by antigen. An antigen is a

foreign substance such as bacterium or virus, that invades the human body. An antibody is a
biochemical molecule hat counteracts a specific antigen.

Classification of Protein Based on Function