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A tetrapeptide has -COOH group on alanin...

A tetrapeptide has `-COOH` group on alanine. This produces glycine (Gly), valine (Val), phenyl alanine (Phe) and alanine (Ala), on complete hydrolysis. For this tetrapeptide, the number of possible sequences (primary structures) with `-NH_(2)` group attached to a chiral centre is :

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Tetrapeptide is made of naturally occuring alanine , serine, glycine and valine . If the C-terminal amino acid is alanine and the N-terminal amino acid is chiral , the number of possible sequences of the tetrapeptide is

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A hexapeptide has the composition Ala,Gly,Phe,Val. Both the N- terminal and C- teminal units are Val. Cleavage of the hexapeptide by chymotypsin gives two different tripeptides, both having Val as the N-terminal group. Among the products of random hydrolysis is a Ala-Val dipeptide fragment . What is the primary structure of the hexapeptide?

Proteins are high molecular mass complex biomolecules of amino acids. The important proteins required for our body are enzymes, hormones, antibodies, transport proteins, structural proteins, contractile proteins etc. Except for glycine, all alpha -amino acids have chiral carbon atom and have L-configuration. The amino acids exists as dipolar ion called zwitter ion, in which a proton goes from the carboxyl group to the amino group. A large number of alpha -amino acids are joined by peptide bonds forming polypeptides. The peptides having very large molecular mass (more than 10,000) are called proteins. The structure of proteins is described as primary structure giving sequence of linking of amino acids, secondary structure giving manner in which polypeptide chains are arranged and folded, tertiary structure giving folding, coiling or bonding polypeptide chains producing three dimensional structures and quaternary structure giving arrangement of sub-units in an aggregate protein meolecule. All proteins on hydrolysis give

GRB PUBLICATION-BIOMOLECULES, POLYMERS, PRACTICAL ORGANIC CHEMISTRY AND CHEMISTRY IN DAILY LIFE-SUBJECTIVE TYPE
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