Chemistry-Viii Notes Prepared by Dr. Dhondiba Vishwanath Suryawanshi, GFGC KR Puram Bengaluru-36
Chemistry-Viii Notes Prepared by Dr. Dhondiba Vishwanath Suryawanshi, GFGC KR Puram Bengaluru-36
UNIT-II
Proteins 5 hours Max. Marks: 12-14
α-amino acids: Introduction, structure (Glycine, Alanine, Valine, Cysteine,
Aspartic acid, Lysine, Tyrosine and proline), classification on the basis of polarity
of R-groups, essential and non-essential amino acids with examples, ionic
properties and reactions of amino acids with alcohol, nitrous acid and Ninhydrin.
Peptides & peptide bond. Levels of organizations of Protein: Primary structure,
Secondary structure (α-helix, β-pleated structure & triple helix-Collagen), tertiary
structure(forces stabilizing tertiary structure) and quaternary structure.
Denaturation and renaturation, Anfinsen’s experiment with ribonuclease.
Classification of proteins based on shape, composition and biological function
(enzymes, hormones, transport agents, structural & antibodies with examples).
2) Structure of alanine:
3) Structure of valine:
4) Structure of Cysteine:
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CHEMISTRY-VIII NOTES PREPARED BY Dr. DHONDIBA VISHWANATH SURYAWANSHI, GFGC KR PURAM BENGALURU-36
6) Structure of lysine:
7) Structure of tyrosine:
8) Structure of proline:
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CHEMISTRY-VIII NOTES PREPARED BY Dr. DHONDIBA VISHWANATH SURYAWANSHI, GFGC KR PURAM BENGALURU-36
Classification of amino acids: Amino acids are classified with different ways
namely based on polarity of side chain group and urge to the growth of the
animal body
I) Classification of amino acids based on the polarity of R (side chain)
groups: Based on the polarity of R (side chain) groups amino acids are
classified into following four categories-
1) Non –polar or hydrophobic R –groups: Those amino acids in which R -
group in α- amino acids are non-polar (do not form positive and negative
charge) are called non-polar or hydrophobic R –groups α- amino acids.
Examples:
Non-polar or hydrophobic R - Name and structure
group
-CH3
(CH3)2CH-
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CHEMISTRY-VIII NOTES PREPARED BY Dr. DHONDIBA VISHWANATH SURYAWANSHI, GFGC KR PURAM BENGALURU-36
-H
-CH2OH
-CH2SH
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CHEMISTRY-VIII NOTES PREPARED BY Dr. DHONDIBA VISHWANATH SURYAWANSHI, GFGC KR PURAM BENGALURU-36
-CH2COO-
-CH2CH2COO-
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CHEMISTRY-VIII NOTES PREPARED BY Dr. DHONDIBA VISHWANATH SURYAWANSHI, GFGC KR PURAM BENGALURU-36
II) Based on the need to the animal for their growth, α-amino acids are
classified into following types
1) Essential amino acids: Those amino acids which are not synthesized in
human (or animal) body, hence they must be supplied in the form of food for
proper growth of human (or animal) are called essential amino acids.
For example: Methionine, lysine, tryptophan, etc.
2) Non-essential amino acids: Those amino acids which are synthesized in
human (or animal) body, hence they not required to supply in the form of
food for proper growth of human (or animal) are called non - essential amino
acids.
For example: Glycine, alanine, serine, etc.
Properties of amino acids:
1) Ionic properties of amino acids: Since amino acids have both amino and
carboxylic acid groups, they are amphoteric in nature. In aqueous solution
near neutral pH, most of the amino acids exist as bipolar molecules with
both positive and negative charges called zwitter ion
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CHEMISTRY-VIII NOTES PREPARED BY Dr. DHONDIBA VISHWANATH SURYAWANSHI, GFGC KR PURAM BENGALURU-36
2) Reaction of amino acids with alcohols: When alpha amino acid is heated
with alcohol in presence of dry hydrochloric acid to form ester derivatives
of alpha amino acids
3) Reaction of amino acids with nitrous acid: When alpha amino acid is
treated with nitrous acid (nitrous acid is obtained by treating sodium nitrite
with dil. Hydrochloric acid at low temperature) at room temperature to
form hydroxyl carboxylic acid with liberation of nitrogen gas.
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CHEMISTRY-VIII NOTES PREPARED BY Dr. DHONDIBA VISHWANATH SURYAWANSHI, GFGC KR PURAM BENGALURU-36
OR
Peptide bond(s): When two or more (n) amino acids undergo condensation
reaction to form the products containing one or (n-1), -CONH- bond(s)
called peptide bond(s).
For examples:
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CHEMISTRY-VIII NOTES PREPARED BY Dr. DHONDIBA VISHWANATH SURYAWANSHI, GFGC KR PURAM BENGALURU-36
Proteins: Polymers of less than twenty five amino acids are called peptides
Polymers of more than twenty five amino acids are called polypeptides Proteins
are polypeptides with molecular mass greater than 10000 with specific function
and biological activities.
Levels (structural) of organization of proteins: Proteins are highly complex
polymers which exhibit unique structural features which enable them to perform
specific functions in cells.
The structure of proteins is explained in four levels of organization.
Primary structure of protein: Primary structure is the unique linear sequence of
amino acids in a protein, from the amino terminus to the carboxyl terminus. The
amino acids are joined together by peptide bonds. The primary structure of a
protein is specified by the sequence of nucleotide bases in the gen that codes for
it. The primary structure therefore determines the properties of proteins and also
specifies its secondary, tertiary and quaternary structures.
Even a single change in the primary structure of a protein may cause drastic
changes in its function, leading to the molecular diseases. The determination of
the amino acid sequence of a protein is difficult task. Frederic Sanger elucidated
the complete amino acid sequence of polypeptide hormone insulin. Insulin was
first protein to be sequenced.
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CHEMISTRY-VIII NOTES PREPARED BY Dr. DHONDIBA VISHWANATH SURYAWANSHI, GFGC KR PURAM BENGALURU-36
form the core, while the R group of the component amino acids extend
outward from the helix. This minimizes steric interference between them.
Though hydrogen bonds are individually weak, so many of them are formed in an
α-helix that they collectively strengthen it considerably. The helix has 3.6 amino
acids per turn, and is right handed i.e. the coils twist clockwise around the axis.
Thus, amino acids 3 to 4 residues apart are brought specially close to each other.
α- helical structures were proposed by Linus Pauling and Robert Corey
from their studies on fibrous proteins. α- keratin consists almost entirely of the α-
helix is also found in globular proteins, where its content varies from almost 0 to
more than 75% of the total chain length. Example- In hemoglobin which is a
globular and flexible proteins, there is about 80% α- helical content.
b) The β-sheet: The β-sheet: This was also proposed by Pauling and Corey.
Fibroin of silk is composed almost entirely of β-sheet structure
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CHEMISTRY-VIII NOTES PREPARED BY Dr. DHONDIBA VISHWANATH SURYAWANSHI, GFGC KR PURAM BENGALURU-36
gel which stiffens the structure. In the transparent cornea of the eye, it is
arranged in a stacked manner that transmits light with minimal scattering. In
bone and skin, collagen fibres are arranged at an angle to each other so as to
resist mechanical shear].
Each of the of the three chains of collagen is about 100 amino acid residues long.
These chains are helices which are twisted around each other to form a rope
liketriple helix, which is called tropocollagen.
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CHEMISTRY-VIII NOTES PREPARED BY Dr. DHONDIBA VISHWANATH SURYAWANSHI, GFGC KR PURAM BENGALURU-36
amino acids long. Thus, the subunit structure of hemoglobin is written as α 2β2. The
arrangement of these four subunit chains with respect to each other is called
quaternary structure of hemoglobin. Its quaternary structure enables it to work
cooperatively, i.e., the binding of oxygen to one subunit increases the affinity of
the other subunits for oxygen.
Denaturation of proteins: Destruction of the three dimensional structure of
protein by heating or by adding reagents( strong acids, strong alkalies, acetones,
alcohols, urea, detergents, organic solvents) or by mechanical shaking or by
passing strong rays which leads to loss of biological activity is called denaturation
of proteins.
Agents of denaturation: Denaturation process can be brought using following
agent
1) Physical agents: Heat, violent shaking, X-ravs, UV radiation.
2) Chemical agents: Acids, alkalis, organic solvents (ether, alcohol), salts of
heavy metals (Pb, Hg), urea, salicylate.
For example: After heating of natural egg, it became insoluble, hard and opaque
Characteristics of denaturation: The following characters of denaturation
1) The native helical structure of protein is lost
2) The primary structure of a protein with peptide linkages remains intact i.e.,
peptide bonds are not hydrolyzed.
3) The protein loses its biological activity.
4) Denatured protein becomes insoluble in the solvent in which it was
originally soluble.
5) The viscosity of denatured protein (solution) increases while its surface
tension decreases.
6) Denaturation is associated with increase in ionizable and sulphydryl groups
of protein. This is due to loss of hydrogen and disulfide bonds.
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