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Q.Proteins are the most abundant biomolecules of the living system. Proteins are the polymers of about twenty different α\alpha-amino acids which are linked by peptide bonds. Ten amino acids are called essential amino acids. In zwitter ionic form, amino acids show amphoteric behaviour as they react both with acids and bases. On the basis of their molecular shape, proteins are classified into two types : Fibrous and Globular proteins. Structure and shape of proteins can be studied at four different levels i.e., primary, secondary, tertiary and quaternary, each level being more complex than the previous one. The secondary or tertiary structure of proteins get disturbed on change of pH or temperature and they are not able to perform their functions. This is called denaturation of proteins. Answer the following questions :

(a) What are essential amino acids ?
(b) What is meant by zwitter ionic form of amino acids ?
(c)
(i) Give one example each for Fibrous protein and Globular protein.
(ii) What type of linkages hold monomers of proteins together ?
(OR)
(c)
(i) What is the structural feature which characterises a reducing sugar ?
(ii) What is the structural difference between nucleoside and nucleotide ?
CBSECBSE Class XII Board 2024Subjective· 4mImportance★★★★★
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(a) Essential amino acids cannot be made by the body; a zwitterion is the dipolar NH3+/COO−NH_3^+/COO^- form of an amino acid (amphoteric); fibrous protein e.g. keratin, globular e.g. insulin; monomers are joined by peptide bonds. (c) A reducing sugar has a free aldehyde/ketone group (free anomeric carbon); a nucleoside is base+sugar while a nucleotide is base+sugar+phosphate.

Part (a)

  1. Essential amino acids. These are the amino acids the human body cannot synthesise (or cannot make fast enough) and must therefore obtain from the diet — for example valine, leucine, isoleucine, lysine, methionine, phenylalanine, threonine and tryptophan.
  2. Zwitterionic form. An amino acid has an acidic −COOH-COOH and a basic −NH2-NH_2 group. In aqueous solution the proton transfers internally from the carboxyl to the amino group, giving a dipolar ion (zwitterion):

    R-CH(NH2)-COOH  ⇌  R-CH(NH3+)-COO−\text{R-CH}(NH_2)\text{-COOH} \;\rightleftharpoons\; \text{R-CH}(NH_3^+)\text{-COO}^-

    The molecule is electrically neutral overall but bears both a positive (NH3+NH_3^+) and a negative (COO−COO^-) charge. Because it has both an acidic and a basic centre, it reacts with both acids and bases — it is amphoteric. (c)(i) Fibrous vs globular examples.
  • Fibrous protein (long, thread-like, insoluble, structural): keratin (also collagen).
  • Globular protein (compact, spherical, soluble, functional): insulin (also haemoglobin, enzymes). …

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