PROTEINS

Proteins are one of the essential building

blocks of the human body.
They provide Amino Acids, Which are a nutritional
requirement of the body to produce its own
proteins and a variety nitrogen-based molecules.
It is common for programs to recommend a minimum
of 50 grams of protein per day to maintain healthy
levels.
Proteins vary in structure as well as function. They are
constructed from a set 20 amino acids and have distinct
three-dimensional shapes.
 Proteins are necklaces of amino acids – long chains molecules.
 Proteins are the basis of how biology get this done. As enzymes, they
are driving force behind all the biochemical reactions which make
biology work.
 As structural elements, they are main constituents of our bones,
muscles, hair, skin, and blood vessels.
 Proteins are organic compounds with a high molecular weight
formed of carbon, oxygen, hydrogen, and nitrogen and may also
contain sulfur, phosphorus coloring non-protein organic groups and
mental ions.
 They are polymers formed of sub-units called amino acids linked
together by Peptide Linkage.
Properties of protein
Solubility- forms colloidal solution instead of true
solutions in water- large size of protein
Molecular weight- depends on number of amino
acid.
Shaped- there is wide variety in shape –
globular(insulin), Oval(albumin), fibrous or
elongated(fibrinogen)
Acidic and Basic- depends on ratio of (lysine
+arginine) : (glut + asp). Ratios greater than 1 is basic
and vise-versa.
Properties of Protein:Charge
Protein are isoelectric
Nature of amino acids determines the pH of a protein.
Acidic amino acid (asp, glu) and basic amino acid (His, lys,
Arg) – determines the charge on protein
At isoelectric pH, the protein exist as Zwitter-Ions and
Dipolar ions.
-Electrically natural
-Minimum solubility
-Maximum precipitability
-Least buffering capacity
Function of Proteins
 Enzymes like trypsin and pepsin help in catalysis of biochemical
reaction.
 Hemoglobin of RBC helps in transporting oxygen from lungs to various
tissues through blood stream and also provide red colour to RBC.
 Myoglobin of muscles stores oxygen until it is needed for energy
pproduction.
 Myosin and Actin are involved in muscle movement.
 Collagen and Keratin Provide structural and protective function in
hairs, teeth, nails, etc..
 Antibodies recognize and destroy foreign bodies which are also protein.
 Casein and Ferritin Stores protein in milk and iron in spleen and liver
respectively.
Another functions of proteins
 Hair and Nails- a protein called alpha-keratin forms your hair and fingernails, and
also is the major component of feathers, wool, claws, scales, horns, and hooves.
 Blood- The hemoglobin protein carries oxygen in your blood to every part of your
body,
 Brain and Nerves- Ion channel proteins control brain signaling by allowing small
molecules into and out of nerve cells
 Muscles- its proteins called actin and myosin enable all muscular movement from
blinking to breathing to roller blading.
 Cellular Mesengers- Receptor proteins stud the outside of your cells and transmit
signals to partner proteins on the inside of the cells.
 Enzymes- enzymes in your saliva, stomach, and small intestine are proteins that
help you digest food.
 Antibodies- are proteins that help defend your body against foreign invaders, such
as bacteria and viruses.
 Cellular Construction Workers- Huge clusters of proteins form molecular
machines that do your cells heavy work, such as copying genes during cell
divisions and making new proteins.
Amino Acid
 It’s a group of organic compounds containing two
functional groups – amino (-NH2) and carboxyl group
(-COOH).

 Its also called Zwitter ion- both Acidic and basic

Functional group (dipolar ion)

 This property is known as amphoteric and are often Called Ampholytes.

 Neither humans nor any other higher animals can synthesize 10 of the 20
common amino acids – Essential Amino Acids.
 Classification
 Amino Acids has been classified under various ways.
- Structures
 With side chain containing Aliphatic Side Chain
 With side chains containing Hydroxylic (OH) groups
 With side chains containing Sulfur Atoms
 With side chains containing Acidic group or Their Amides
 With side chains containing Basic Groups
 Containing Aromatic Rings
 Imino acids

-Polarity
 Non Polar
 Polar

-Nutritional
 Essential and Non essential
Definition
Essential amino acids are the amino
acids which have to be take in
through diet as they “CAN NOT” be
produced by the body.
There are 9 amino acids out of 20
are thought to be essentials
serves to build and repair muscle
tissues. Also, it forms precursor
molecules for the formation of
neurotransmitters in the brain.
Highly probably as these amino acids
are acquired through food.
Non-essential amino acids need not
be taken in through diet as they can
be produced by the body.
11 Of the 20 amino acids are non-
essential.
Removal of toxins integral in the
synthesis of RBC and WBC promotes
brain function and many more.
Probability of deficiency is rare, but
can still occur due to starvation or
illness.
Side chains containing Hydroxylic (OH)
groups
Containing Aromatic Rings
Side chain containing Aliphatic Side Chains
Simplest amino
acids .

Contains branched
chain of
hydrocarbons.
Structures of Protein
Proteins catalyze metabolic reactions, power cellular
motion, and forms structural integrity to hair, bones,
tendons and teeth.
Human Proteins therefore reflects the sophistication and
diversity of their biologic roles.
Therefore maturation of a newly systhesized polypeptide
into a biologically functional protein.
- Requires folding into a specific three-dimensional
arrangement, or Conformation.
Levels of Protein Organization
-The modular nature of proteins synthesis and folding are embodied in
the concept of orders of protein structures:
 Primary structure- the sequence of amino acids in the polypeptide
chain.
 Secondary structure- the formation of a helices and B pleated sheets
due to hydrogen bonding between the peptide backbone.
 Tertiary structure- Folding of helices and sheets influenced by R
group bonding.
 Quarternary Structure- The association of more than one
polypeptide into a protein complex influenced by R group bonding.
Primary Structure
 Primary(1) structure
 Each protein has a distinctive number and sequence
of amino acids.

 These determines how it folds up into

a unique three- dimensional structure.

 This in turn determines the function

of the protein.
Secondary Structure
 Polypeptide chain can arrange itself into characteristic Helical or
pleated segments
-Given by pauling and corey
-Hydrogen bonding interactions between
adjacent amino acids residues.

 Free rotation is possible about only two

of the three covalent bonds of the
polypeptide backbone.
-a-carbon (Ca) to the carbonyl carbon (Co)
bond.
-Ca to nitrogen bonds
Tertiary structure
 Single domain- Triose phosphate isomerase, myoglobin
 Two domain- Lactate dehydrogenase, quinone axidoreductase.
 A polypeptide with 200 amino acids
normally consist of two or more domains.

Tetrameric enzyme lactate

Dehydrogenase with the substrates
NaDh (red) and pyvate (blue) bound
Quarternary Structures
 Marjority of proteins are composed of single polypeptide chains.
 Some of protein consist of 2 or more polypeptide chain which may be
identical or different.
 Such protein are termed as oligomers and poses quarternary structures.
 When it consists of 2 polypeptides - dimers
 Homodimers Contain two copies of the same polypeptide chain, while in a
heterodimer the polypeptides differ.
Denaturation
The phenomenon of disorganization of Native protein
structure
It results in the lost of secondary, tertiary and quarternary
structure of proteins
It involves the change of physical, chemical and biological
properties
Agents of Denaturation
-Physical agents: Heat, UV radiationn, X-rays and violent shaking
(centrifuge)
-Chemical agents: acids, alkanes, organic solvents (ether, alcohol), salts
of heavy metals, urea, salicylate
Denaturation
Coagulation
-Irreversible denaturation of protein to semi- solid viscous
precipitate
-albumins and globulins – coagulable proteins
Flocculation
-protein precipitation at isoelectric pH
-Precipitate is known as flocculum
-Casein – milk protein, prepared by adjusting isoelectric pH
by dilute acetic acid
-Its reversible, but on heating it turns to be irreversible
Denaturation
Primary structures remains intact i.e peptide linkage
are not broken
Loses its biological activity
Insolu ble in solvent which was previously
soluble
Viscosity increases while its surface tension decreases
Its more easily digestible
Its usually Irreversible, but careful denaturation
(renaturation) is reversible
Ex. Hemoglobin is renatured on removal of salicylates.
Renaturation
Renaturation is the conservation of a protein into its native 3D
structure.
Renaturation is basically
the reverse of denaturation.
It involves the reconstruction
of a protein into its original
tertiary structure aftyer denaturation.
The protein once again regains
its biological activity.
Classification of proteins
Based on composition:
 Simple Proteins- composed of entirely amino acids only.
ex. albumin, globulin
 Complex or conjugated proteins – ma;de up of amino acids an`d
other organic compounds. The non-amino acid group is termed as the
prosthetic group.
Ex. Nucleoproeins, lipoproteins,
glycoproteins and metalloproteins
Classification of proteins
Based on Axial Ratio
Axial Ration is the ratio of the length to the breath.
 Globular Proteins- with the axial ratio less than 10 but not below 3 or
4. They are compactly folded and coiled.
Ex. Insulin, Plasma albumin, Globulin, Enzymes
 Fibrous Proteins- with axial ratio greater
than 10. they are spiral and helical and
are cross linked by disulfide and
hydrogen bonds.
Ex. Keratin, myosin, elastin, collagen
Aliphatic functional groups
Aliphatic compounds are those hydrocarbons that are the open
chain compounds and also closed chain
They can be saturated as well as unsaturated where the system
can be open as well as closed chain.
Usually they are of the three types based on the number of
bonds between them that is single bonded aliphatic compounds
are called alkanes, double bonded are the alkanes and triple
bonded are the alkanes.
A functional group attached to these compounds are aliphatic
functional groups.
Example of an a aliphatic compounds are methane, propane,
butane, etc…
Aromatic functional group
Aromatic compound are those who have only a closed chain
structure.
They are the special classes of unsaturated hydrocarbon which
is based on the six carbon moietis that is called banzeze,
They are also called as arenes or aromatic and the compounds
are having a conjugated planar ring system which is further
accompanied by delocalised pi- electron that is alternating
double and single bonds.
A functional group attached to these compounds are aromatic
functional groups.
Examples for aromatic compound are benzene, toluene, etc…
Peptide bond
 Within a protein, multiple amino acids are linked together by bonds,
thereby forming a long chain.

 Peptide bonds are formed be a

biochemical reaction that extracts a
water molecule as it joins the amino
acids group of one amino acids to the
carboxyl group of a neighboring.
Biological function of protein
 Structural Protein; Collagen, elastin, keratin, fibroin of silk and webs.
 Transport Protein: Hemoglobin, myoglobin, lipoproteins
 Protective Proteins: Immunoglobulins, fibrinogen, thrombin, snake
venoms, bacterial toxins.
 Contractile Proteins: actin, myosin, tubulin
 Catalytic Proteins: enzymes
 Regulatory proteins: hormones
 Storage proteins: ferritin, hemosiderin, gluten, casein, ovalbumin
 Reception of stimuli: rhodopsin, membrane receptor proteins,
acethylcholine, insulin
 Germicidal Proteins: Polymyxin B1, Gramicidin S
Clinical significance
Blood purification procedure.
Protein is an essential component of protoplasm.
Both structure and function of body tissues are dependent
on specific proteins, such an enzymes and hormones.
Fluid balance, hemostasis, many hormone and lipoprotein
complexes and certain immune mechanisms are related to
protein nutrition.
Immune system attacts body’s own tissue.
Effective for temporary treatment of autoimmune disease.
Thank you!!
Fighting!!