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NCERT Solutions For Class 11 Biology Biomolecules
NCERT Solutions Class 11 Biology Biomolecules
NCERT Solutions For Class 11 Biology Biomolecules is designed and prepared by the best teachers across India. All the important topics are covered in the exercises and each answer comes with a detailed explanation to help students understand concepts better. These NCERT solutions play a crucial role in your preparation for all exams conducted by the CBSE, including the JEE.
NCERT TEXTBOOK QUESTIONS SOLVED
1. What are macromolecules ? Give examples.Ans. Macromolecules are large high molecular weight substances with complex molecular structure and occur in colloidal state (being insoluble) in intracellular fluid. These are formed by polymerisation of large number of micromolecules. Polysaccharides, proteins and nucleic acids are few examples.
2. Illustrate a glycosidic, peptide, and a phospho- diester bond.Ans. (i) Glycosidic bond is the type of chemical linkage between the monosaccharide units of disaccharides, oligosaccharides and polysaccharides, which is formed by the removal of a molecule of water.
(ii)Peptide bonds are formed by the reaction between carboxyl (- COOH) of one amino acid and amino (- NH2) group of other amino acid with the elimination of water.
(iii) In a polynucleotide chain, adjacent nucleotides are joined together by a bond called phosphodiester bond. This bond links a phosphate group and sugar group of two adjacent nucleotides by means of an oxygen bridge.
Ans. The helical polypeptide molecule may fold on itself and assume a complex but specific form-spherical, rod-like or any form in between these. These geometrical shapes,are known as tertiary (3°) structure of protein molecules. The coils and folds of the polypeptide molecules are so arranged as to hide the non-polar amino acid chains inside and to expose the polar side chains. The tertiary structure of a protein brings distant amino acid side chains nearer to form active sites of enzymatic proteins. The tertiary structure is maintained by weak bonds such as hydrogen, ionic, disulphide and hydrophilic – hydrophobic bonds, formed between one part of a polypeptide and another. This structure is easily disrupted by pH, temperature and chemicals stopping the function of proteins.
4. Find and write down structures of 10 interesting small molecular weight biomolecules.Ans. Interesfing small molecular weight biomolecules are minerals (like sodium, potassium, calcium, zinc, iodine etc), gases (like Oz, N2, C02, NH3) sugars – (ribose, deoxyribose, glucose, fructose), lipids, amino acids, nucleotides (pyrimidines & purine). Structures of 10 interesting small molecular weight biomolecules are as follows:
5. Proteins have primary structure. If you are given a method to know which amino acid is at either of two termini (ends) of a protein, can you connect this information to purity or homogeneity of a protein?Ans. There are several methods provided by several scientists to find out the sequence of amino acids. Frederick Sanger proposed Sanger’s reagent to know the amino acid sequence in a polypeptide chain.
Sanger used 1-fluoro 2, 4 dinitrobenzene (FD NB) to determine insulin structure. FDNB specifically binds with N-terminal amino acid to form a dinitrophenyl (DNP) derivative of peptide. This DNP- derivative peptide can be identified by chromatography. The identified sequence of amino acids shows the homogeneity of a protein molecule.
Ans. Proteins used as therapeutic agents are: thrombin, fibrinogen, enkephalins, antigens, antibodies, streptokinase, protein tyrosine kinase, diastase, renin, insulin, oxytocin, vasopressin etc. Proteins are also used in cosmetics, dairy industries, textile industries, research techniques, biological buffers etc.
7. Can you describe what happens when milk is converted into curd or yoghurt, from your understanding of proteins.Ans.Milk is converted into curd or yoghurt due to denaturation of proteins. In denaturation, disruption of bonds that maintains secondary and tertiary structure leads to the conversion of globular proteins into fibrous proteins. This involves a change in physical, chemical and biological properties of protein molecules.
8. Can you attempt building models of biomolecules using commercially available atomic models (Ball and stick models).Ans. Yes, models of biomolecules can be prepared using commercially available atomic models.
Ball and stick models and space filling models are 3D or spatial molecular models which serve to display the structure of chemical products and substances or biomolecules. With ball and stick models, the centers of the atoms are connected by straight lines which represent the covalent bonds. Double and triple bonds are often represented by springs which form curved connections between the balls. The bond angles and bond lengths reflect the actual relationships, while the space occupied by the atoms is either not represented at all or only denoted essentially by the relative sizes of the spheres.
Ans. The existence of different ionic forms of amino acids can be easily understood by the titration curves. The number of dissociating functional group is one in case of neutral and basic amino acids and two in case of acidic amino acids.
10. What are gums made of ? Is fevicol different ?Ans. Gums are hetero-polysaccharides (poly-mers) of large number of different monosac-charide units. Yes, fevicol is a different kind of polymer. It is a synthetic sticky substance called resin which is manufactured by esteri-fication of organic compounds.
11. Find out how much cellulose is made by all the plants in the biosphere.Ans. About 100 billion tonnes of cellulose is prepared per year by the plants of the world.
12. Describe the important properties of enzymes.Ans. The important properties of enzymes are as follows:
(i) The enzymes are generally proteins which are high molecular weight complex globular proteins. They can associate with non-protein substance for their activity.
(ii) The enzymes do not start a chemical reaction but only accelerate it. They combine temporarily with the substrate molecules and are not consumed or changed permanently in the reaction which they catalyse.
(iii) The enzyme controlled reactions are reversible.
(iv) The enzymes are specific in action. An enzyme catalyses only a particular kind of reaction or acts on a particular substrate only.
(v) The enzymes are thermolabile i.e., heat sensitive and can function best at an optimum temperature. Similarly, enzymes show maximum activity at optimum pH.
(vi) The enzymes are inactivated by poisons and radiation
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