BIOCHEMISTRY
module 6b:
proteins
Presented by AJRJ Group
Our Team
Alesandra Nicole Alcantara
Jeremy Catuar
Rommel Navelgas
Justine Brenan Talla
At the end of this module, the students should be able to:
a. define protein and describe their functions;
b. differentiate primary, secondary, tertiary and quaternary proteins;
c. explain the properties of proteins - including its solubility, molecular
weight, shape, isoelectric ph, acidic and basic of protein,
precipitation of protein, and colour reaction of proteins;
d. classify processes that change the structure or aggregation state of
proteins- including denaturation, coagulation, and flocculation; and
e. discuss the classification of protein based on function, chemical
nature and solubility properties and nutritional.
WHAT ARE PROTEINS?
- are the most abundant organic molecules of the living system. They occur
in every part of the cell and constitute about 50% of the cellular dry
weight. Proteins form the fundamental basis of structure and function of
life.
-The term protein is derived from a Greek word proteios, meaning holding
the first place. Berzelius (Swedish chemist) suggested the name proteins to
the group of organic compounds that are utmost important to life. Mulder
(Dutch chemist) in 1838 used the term proteins for the high molecular
weight nitrogenrich and most abundant substances present in animals and
plants.
FUNCTIONS OF PROTEINS
Static/Structural Function
-Certain proteins perform brick and mortar roles and are primarily responsible for
structure and strength of body. These include collagen and elastin found in bone
matrix, vascular system and other organs and α-keratin present in epidermal
tissues.
Dynamic Function
-The dynamic functions of proteins are more diversified in nature. These include
proteins acting as enzymes, hormones, blood clotting factors, immunoglobulins,
membrane receptors, storage proteins, besides their function in genetic control,
muscle contraction, respiration etc. Proteins performing dynamic functions are
appropriately regarded as the working horses of celL.
PEPTIDE BOND
PRIMARY PROTEIN The amino acids are held together in a protein by covalent
peptide bonds or linkages. These bonds are rather strong and
serve as the cementing material between the individual amino
refers to the linear sequence of acids (considered as bricks).
amino acids in the polypeptide
Formation of a peptide bond
chain. These amino acids are
When the amino group of an
joined together by peptide
amino acid combines with the
bonds, which are covalent
carboxyl group of another amino
bonds formed between the
carboxyl group of one amino acid, a peptide bond is formed.
acid and the amino group of Note that a dipeptide will have
the next. two amino acids and one
peptide (not two) bond. Peptides
containing more than 10 amino
acids (decapeptide) are referred
to as polypeptides.
1. Alpha Helix:
SECONDARY PROTEINS
AND ITS TWO TYPES - Structure: Imagine a coiled spring. That's what an
alpha helix looks like. It's a right-handed helix, meaning it
twists clockwise when viewed from the top. The
The conformation of polypeptide chain
by twisting or folding is referred to as polypeptide chain spirals around a central axis, with the
secondary structure. The amino acids R groups (side chains) of the amino acids pointing
are located close to each other in their
outwards.
sequence. Two types of secondary
structures, α-helix and β-sheet, are - Examples: Keratin, found in hair and nails, is rich in
mainly identified. Indian scientist alpha helices.
Ramachandran made a significant
contribution in understanding the
spatial arrangement of polypeptide
chains.
2. Beta Pleated Sheet: -β-Pleated sheet may be formed either by
separate polypeptide chains (H-bonds are
- Structure: Imagine a folded sheet of paper. A beta sheet
interchain) or a single polypeptide chain
is similar, but it's formed by two or more polypeptide chains
folding back on to itself (H-bonds are
that lie side-by-side. These chains are called beta strands.
intrachain).
The strands are held together by hydrogen bonds between
the backbone atoms of adjacent strands.
Occurrence of β-sheets
Many proteins contain β-pleated sheets. As
THERE ARE TWO TYPES
such, the α-helix and β-sheet are commonly
- PARALLEL: Beta strands run in the same direction (N-
terminus to C-terminus). found in the same protein structure In the
- ANTI-PARALLEL: Beta strands run in opposite directions. globular proteins, β-sheets form the core
- Examples: Silk is made of beta sheets, giving it its structure.
smooth, strong texture.
Parallel and anti-parallel β-sheets
The polypeptide chains in the β-sheets may be arranged
either in parallel (the same direction) or anti-parallel
(opposite direction).
TerTIARY PROTEINS QUATERNARY PROTEINS
The three-dimensional arrangement of protein A great majority of the proteins are composed of
structure is referred to as tertiary structure. It is a single polypeptide chains. Some of the proteins,
compact structure with hydrophobic side chains however, consist of two or more polypeptides which
held interior while the hydrophilic groups are on the may be identical or unrelated. Such proteins are
surface of the protein molecule. This type of termed as oligomers and possess quaternary
arrangement ensures stability of the molecule. structure. The individual polypeptide chains are known
as monomers, protomers or subunits. A dimer
Bonds of tertiary structure consists of two polypeptides while a tetramer has
Besides the hydrogen bonds, disulfide bonds (–S–S), four.
Bonds in quaternary structure
ionic interactions (electrostatic bonds), hydrophobic
The monomeric subunits are held together by
interactions and van der Waals forces also
nonconvalent bonds namely hydrogen bonds,
contribute to the tertiary structure of proteins.
hydrophobic interactions and ionic bonds.
.
properties of protein
SOLUBILITY MOLECULAR WEIGHT SHAPE
•The proteins vary in their
molecular weights, which, in There is a wide variation
Proteins form colloidal turn, is dependent on the in the protein shape. It
solutions instead of true number of amino acid residues. may be globular (insulin),
solutions in water. This is Each amino acid on an average oval (albumin) fibrous or
due to huge size of protein contributes to a molecular elongated (fibrinogen).
molecules. weight of about 110.
•A few proteins with their Albumin
molecular weights are listed:
Insulin
Insulin-5,700;
Myoglobin-17,000;
Hemoglobin- 64,450; Fibrinogen
Serum albumin- 69,000..
ISOELECTRIC PH
ACIDIC AND BASIC PRECIPITATION OF
The nature of the amino acids PROTEINS PROTEINS
(particularly their ionizable groups)
•Proteins in which the •Proteins exist in colloidal
determines the pI of a protein. The
acidic amino acids (Asp, Glu) and
ratio (ε Lys + ε Arg)/(ε solution due to hydration of
basic amino acids (His, Lys, Arg) Glu + ε Asp) is greater polar groups (-COO-, -NH3+,
strongly influence the pI. At than 1 are referred to as -OH). Proteins can be
isoelectric pH, the proteins exist as basic proteins. precipitated by dehydration
Zwitterions or dipolar ions. They or neutralization of polar
are electrically neutral (do not groups.
migrate in the electric field) with • For acidic proteins,
minimum solubility, maximum the ratio is less than 1.
precipitability and least buffering
capacity. The isoelectric pH(pI) for
some proteins are given here:
7. COLOUR REACTIONS
OF PROTEINS:
The proteins give
several colour
reactions which are
often useful to
identify the nature
of the amino acids
present in them.
Biuret test is answered by compounds containing two or more CO–NH
bIURET REACTION groups i.e., peptide bonds. All proteins and peptides possessing at least
two peptide linkages i.e., tripeptides (with 3 amino acids) give positive
biuret test.
Biuret is a compound Histidine is the only amino acid that answers biuret test. The principle of
biuret test is conveniently used to detect the presence of proteins in
formed by heating urea
biological fluids. The mechanism of biuret test is not clearly known. It is
to 180°C. believed that the colour is due to the formation of a copper co-
ordinated complex, as shown below.
When biuret is treated
with dilute copper
sulfate in alkaline
medium, a purple colour
is obtained. This is the
basis of biuret test
widely used for
identification of proteins
and peptides.
2. The primary structure of a protein with peptide linkages remains
DENATURATION intact i.e.,
The phenomenon of disorganization of native protein 3. The protein loses its biological activity.
structure is known as denaturation. Denaturation 4. Denatured protein becomes insoluble in the solvent in which it
results in the loss of secondary, tertiary and quaternary was originally soluble.
structure of proteins. This involves a change in physical, 5. The viscosity of denatured protein (solution) increases while its
chemical and biological properties of protein surface tension decreases.
molecules. 6. Denaturation is associated with increase in ionizable and
AGENTS OF DENATURATION sulfhydryl groups of protein. This is due to loss of hydrogen and
Physical agents: Heat, violent shaking, X-rays, UV disulfide bonds.
radiation. 7. Denatured protein is more easily digested. This is due to
Chemical agents: Acids, alkalies, organic solvents increased exposure of peptide bonds to enzymes. Cooking causes
(ether, alcohol), salts of heavy metals (Pb, Hg), urea, protein denaturation and, therefore, cooked food (protein) is more
salicylate, detergents (e.g. sodium dodecyl sulfate). easily digested. Further, denaturation of dietary protein by gastric
HCl enchances protein digestion by pepsin.
CHARACTHERISTICS OF DENATURATION 8. Denaturation is usually irreversible. For instance, omelet can be
1. The native helical structure of protein is lost. prepared from an egg (protein-albumin) but the reversal is not
possible.
9. Careful denaturation is sometimes reversible (known as
renaturation). Hemoglobin undergoes denaturation in the presence
of salicylate. By removal of salicylate, hemoglobin is renatured.
10. Denatured protein cannot be crystallized.
COAGULATION FLOCCULATION
The term ‘coagulum’ refers to It is the process of protein
a semi-solid viscous precipitation at isoelectric pH.
precipitate of protein. The precipitate is referred to
Irreversible denaturation as flocculum. Casein (milk
Lorem ipsum dolor sit
results in coagulation.
protein) amet,can consectetur
be easily
Coagulation is optimum and adipiscing
precipitated when elit. Cras to
adjusted
requires lowest temperature at elementum mi sit amet
isoelectric pH (4.6) by dilute
isoelectric pH. Albumins and posuere suscipit. In
globulins (to a lesser extent) acetic varius
acid. risus
Flocculation
a molestie is
are coagulable proteins. Heat reversible. On application of
pellentesque.
coagulation test is commonly heat, flocculum can be
used to detect the presence of converted into an irreversible
albumin in urine. mass, coagulum.
CLASSIFICATION OF PROTEIN
Proteins are classified in several ways. Three major types of classifying
proteins based on their function, chemical nature and solubility
properties and nutritional.
A. Functional classification of proteins
Based on the functions they perform, proteins are classified into the following groups
(with examples)
1. Structural proteins :
Keratin of hair and nails- fibrous structural protein of hair, nails, horn, hoofs, wool,
feathers, and of the epithelial cells in the outermost layers of the skin. Keratin serves
important structural and protective functions, particularly in the epithelium.
Collagen of bone - is principal protein of the skin, tendons, ligaments, cartilage, bone,
and connective tissue.
2. Enzymes or catalytic proteins
Hexokinase- is a type of sugar kinase that plays a key role in the phosphorylation of glucose, which is
the initial step in glucose metabolism.
Pepsin- the powerful enzyme in gastric juice that digests proteins such as those in meat, eggs, seeds,
or dairy products.
3. Transport proteins :
Hemoglobin- is a complex iron-containing protein found in erythrocytes (red blood cells) of most
vertebrates that plays a vital role in carrying oxygen and carbon dioxide within the blood. It is also the
component that makes our blood red.
Serum albumin- most abundant circulating plasma protein. It constitutes about half of the total protein
content (3.4 to 5.4 g/dL) of the plasma (i.e., component of blood without blood cells).
4. Hormonal proteins :
Insulin-hormone that regulates the level of sugar (glucose) in the blood and that is produced by the
beta cells of the islets of Langerhans in the pancreas. Insulin is secreted when the level of blood
glucose rises—as after a meal.
Growth hormone-peptide hormone produced by the pituitary gland, that stimulates development,
growth, and regeneration.
5. Contractile proteins :
Actin- protein that is an important contributor to the contractile property of muscle
and other cells. It exists in two forms: G-actin (monomeric globular actin) and F-actin
(polymeric fibrous actin), the form involved in muscle contraction.
Myosin- motor protein found in muscle cells that, through its interaction with actin,
plays a crucial role in muscle contraction and movement. It converts chemical energy
in the form of ATP to mechanical energy, thus enabling the muscles to contract.
6. Storage proteins :
Ovalbumin-major protein component of egg white, representing 45% of the total
proteins. It undergoes a conversion into a de-aminated form known as S-ovalbumin,
which is used as a marker for egg freshness and can affect the processing conditions
of egg-based products.
Glutelin- globular protein categorized within the prolamin proteins group, is
commonly distributed among cereal grains, notably in wheat, barley, and rice.
7. Genetic proteins :
Nucleoproteins- molecule consisting of a protein linked to a nucleic acid, either DNA
(deoxyribonucleic acid) or RNA (ribonucleic acid).
8. Defense proteins :
Snake venoms- mixture of peptides and proteins that evolved to disrupt physiological
pathways in a prey item but also severely affects humans during defensive snakebites.
Immunoglobulins- is a protein produced by the B cell of the immune system that
functions as an antibody to defend the body against pathogens.
9. Receptor proteins for
Hormones- is a receptor protein on the surface of a cell or in its interior that binds to a
specific hormone. The hormone causes many changes that take place in the cell.
Viruses-viral attachment protein can be viewed as the “key” that unlocks host cells by
interacting with the “lock”—the receptor—on the cell surface, and these lock-and-key
interactions are critical for viruses to successfully invade host cells.
B. Protein classification based on
chemical nature and solubility
This is a more comprehensive and popular
classification of proteins. It is based on the
amino acid composition, structure, shape and
solubility properties. Proteins are broadly
classified into 3 major groups
1. Simple proteins : They are composed of only
amino acid residues.
2. Conjugated proteins : Besides the amino
acids, these proteins contain a non protein
moiety known as prosthetic group or conjugating
group.
3. Derived proteins : These are the denatured
or degraded products of simple and conjugated
proteins.
simple proteins
A. Globular proteins : These are spherical or
oval in shape, soluble in water or other solvents
and digestible.
(i) Albumins : Soluble in water and dilute salt
solutions and coagulated by heat. e.g. serum
albumin, ovalbumin (egg), lactalbumin (milk).
(ii) Globulins : Soluble in neutral and dilute salt
solutions e.g. serum globulins, vitelline (egg
yolk).
(iii) Glutelins : Soluble in dilute acids and
alkalies and mostly found in plants e.g. glutelin
(wheat), oryzenin (rice).
(iv) Prolamines : Soluble in 70%
alcohol e.g. gliadin (wheat), zein
(maize).
(v) Histones : Strongly basic proteins,
soluble in water and dilute acids but
insoluble in dilute ammonium
hydroxide e.g. thymus histones.
(vi) Globins : These are generally
considered along with histones.
However, globins are not basic
proteins and are not precipitated by
NH4OH.
(vii) Protamines : They are strongly basic
and resemble histones but smaller in size
and soluble in NH4 OH. Protamines are also
found in association with nucleic acids e.g.
sperm proteins.
(viii) Lectins are carbohydrate-binding
proteins, and are involved in the interaction
between cells and proteins. They help to
maintain tissue and organ structures. In the
laboratory, lectins are useful for the
purification of carbohydrates by affinity
chromatography e.g. concanavalin A,
b. fibrous proteins
These are fiber like in shape, insoluble in water
and resistant to digestion. Albuminoids or
scleroproteins are predominant group of fibrous
proteins.
(i) Collagens are connective tissue proteins
lacking tryptophan. Collagens, on boiling with
water or dilute acids, yield gelatin which is soluble
and digestible.
(ii) Elastins : These proteins are found in elastic
tissues such as tendons and arteries.
(iii) Keratins : These are present in exoskeletal
structures e.g. hair, nails, horns. Human hair keratin
contains as much as 14% cysteine.
CONJUGATED PROTEINS
(a) Nucleoproteins : Nucleic acid (DNA or
RNA) is the prosthetic group e.g.
nucleohistones, nucleoprotamines.
(b) Glycoproteins : The prosthetic group is
carbohydrate, which is less than 4% of
protein. The term mucoprotein is used if the
carbohydrate content is more than 4%. e.g.
mucin (saliva), ovomucoid (egg white).
(c) Lipoproteins : Protein found in
combination with lipids as the prosthetic
group e.g. serum lipoproteins.
(d) Phosphoproteins: Phosphoric
acid is the prosthetic group e.g.
casein (milk), vitelline (egg yolk).
(e) Chromoproteins:
The prosthetic group is coloured in
nature e.g. hemoglobins,
cytochromes.
(f) Metalloproteins:
These proteins contain metal ions
such as Fe, Co, Zn, Cu, Mg etc., e.g.
ceruloplasmin (Cu), carbonic
anhydrase (Zn).
DERIVED PROTEINS (iii) Metaproteins : These are the second stage
The derived proteins are of two types. The products of protein hydrolysis obtained by
primary derived are the denatured or treatment with slightly stronger acids and
coagulated or first hydrolysed products of alkalies e.g. acid and alkali metaproteins.
proteins. The secondary derived are the
degraded (due to breakdown of peptide
bonds) products of proteins.
PRIMARY DERIVED
(i) Coagulated proteins : These are the (b) Secondary derived proteins : These are the
denatured proteins produced by agents such progressive hydrolytic products of protein
as heat, acids, alkalies etc. e.g. cooked hydrolysis. These include proteoses, peptones,
proteins, coagulated albumin (egg white). polypeptides and peptides.
(ii) Proteans : These are the earliest products
of protein hydrolysis by enzymes, dilute acids,
alkalies etc. which are insoluble in water. e.g.
fibrin formed from fibrinogen.
C. Nutritional classification of proteins
complete proteins
These proteins have all the ten essential amino acids in
the required proportion by the human body to promote
good growth. e.g. egg albumin, milk casein.
partially incomplete proteins
These proteins partially lack one or more essential
amino acids, and can promote moderate growth. e.g.
wheat and rice proteins (limiting Lys, Thr).
incomplete proteins
These proteins completely lack one or more essential
amino acids. Hence they do not promote growth at all
e.g. gelatin (lacks Trp), zein (lacks Trp, Lys).
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Thank
You!