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When we talk functional macromolecules (...

When we talk functional macromolecules ( e.g., proteins as enzymes, hormones, receptors, antibodies etc. ), towards what are they evolving ?

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We talk about structural and functional diversification of the macromolecules
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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

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. Which of the following alpha -amino acid does not form optical isomers?

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. Which of the following statements is not correct?

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