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Assignment
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Group-02
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Introduction
1. Amino acids are building blocks of proteins
Definition
An organic compound containing an amino group (NH2),a carboxylic acid
group(COOH),and any of various side groups, especially any of 20
compounds that have the basic formula NH2CHRCOOH,and that link together
by peptide bonds to form proteins or that function as chemical messengers
and as intermediates in metabolism.
1. Non-polar ((Hydrophobic)
2. Polar (Hydrophilic)
c. Un-charged R group
b. Generally unreactive.
Glycine is the simplest amino acid having single H atom as its side chain
Alanine, Valine, Leucine and Isoleucine have saturated hydrocarbon R
groups. Leucine and Isoleucine are isomers of each other.
Proline is rather an amino acid than amino acid because its side chain is
bonded to the backbone Nitrogen as well as to the alpha carbon Phenylalanyl
and Alanine with an extra benzene group on the end side times called phenyl
group.
They confirm a-ve charge on the protein of which they are a part.
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1. Isoleucine
2. Leucine
3. Lysine
4. Methionine
5. Phenylalanine
6. Threonine
7. Tryptophan
8. Valine
The body can make these amino acids from the above essential amino acids.
1. Alanine
2. Arginine
3. Asparagine
4. Aspartic acid
5. Cysteine
6. Glutamic acid
7. Glutamine
8. Glycine
9. Histidine
10. Proline
11. Serine
12. Tyrosine
These are essential for infant, since their bodies cannot produce them yet.
carboxyl group of the second amino acid. The dipeptide formed is followed by the
loss of water. A chain of amino acids are connected by peptide chain while each
individual amino acid is referred to as a residue. These chain then fold due to
various internal and external forces in order to become proteins.
Reaction mechanism:
This reaction to form peptide bonds involve reacting the amine group of one amino
acid to the carboxyl group of another amino acid .A peptide bond is dehydration
reaction or condensation reaction meaning it releases a molecule of water though
the cause of the reaction. The molecule formed by a peptide bond is called an
amide.
Protein denaturation:
Denaturation is a process in which proteins or nucleic acids lose the quaternary
structure, tertiary structure and secondary structure which is present in their native
state by application of some external stress or compound such as a strong acid or
base, a concentrated inorganic solvent. Denaturation the breakdown the bond
forming the quaternary , tertiary and secondary structure of proteins and nucleic
acids.
1. Primary structure: The linear structure of amino acids in the polypeptide chain
3. Tertiary structure: Three dimensional structure alpha helix and beta helixes
folded.
Enzyme kinetics:
Enzyme kinetics is the study of the chemical reaction that catalyzed by enzyme. In
enzyme kinetics the reaction rate is measured and the effects of varying the
condition of the reaction are investigated. Its role in metabolism how its activity is
control, how a drug or an agonist might inhibit the enzyme. Enzymes are usually
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