NCERT Solutions Class 11 Biology Chapter 9 Biomolecules – Here are all the NCERT solutions for Class 11 Biology Chapter 9. This solution contains questions, answers, images, explanations of the complete chapter 9 titled Biomolecules of Biology taught in Class 11. If you are a student of Class 11 who is using NCERT Textbook to study Biology, then you must come across chapter 9 Biomolecules. After you have studied lesson, you must be looking for answers of its questions. Here you can get complete NCERT Solutions for Class 11 Biology Chapter 9 Biomolecules in one place.
NCERT Solutions Class 11 Biology Chapter 9 Biomolecules
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For a better understanding of this chapter, you should also see summary of Chapter 9 Biomolecules , Biology, Class 11.
NCERT Solutions Class 11 Biology chapter 9 Biomolecules
Class 11, Biology chapter 9, Biomolecules solutions are given below in PDF format. You can view them online or download PDF file for future use.
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Question & Answer
Q.1: What are macromolecules? Give examples.
Ans : Macromolecules are large complex molecules that occur in colloidal state in intercellular fluid. They are formed by the polymerization of low molecular weight micromolecules. Polysaccharides, and nucleic acids are common examples of macromolecules.
Q.2: Illustrate a glycosidic, peptide and a phosphodiester bond.
Ans : (a) Glycosidic bond is formed normally between carbon atoms, 1 and 4, of neighbouring monosaccharide units. (b) Peptide bond is a covalent bond that joins the two amino acids by - NH - CO linkage. (c) Phosphodiester bond is a strong covalent bond between phosphate and two sugar groups. Such bonds form the sugar phosphate backbone of nucleic acids.
Q.3: What is meant by tertiary structure of proteins?
Ans : The helical polypeptide chain undergoes colling and folding to form a complex three-dimensional shape referred to as tertiary structure of proteins. These coils and folds are arranged to hide the non-polar amino acid chains and to expose the polar side chains. The tertiary structure is held together by the weak bonds formed between various parts of the polypeptide chain.
Q.4: Find and write down structures of 10 interesting small molecular weight biomolecules. Find if there is any industry which manufactures the compounds by isolation. Find out who are the buyers.
Ans : (a) (b)
Q.5: Proteins have primary structure. If you are given a method to know which amino acid is at either of the two termini (ends) of a protein, can you connect this information to purity or homogeneity of a protein?
Ans : Yes, if we are given a method to know the sequence of proteins, we can connect this information to the purity of a protein. It is known that an accurate sequence of a certain amino acid is very important for the functioning of a protein. If there is any change in the sequence, it would alter its structure, thereby altering the function. If we are provided with a method to know the sequence of an unknown protein, then using this information, we can determine its structure and compare it with any of the known correct protein sequence. Any change in the sequence can be linked to the purity or homogeneity of a protein. For example, any one change in the sequence of haemoglobin can alter the normal haemoglobin structure to an abnormal structure that can cause sickle cell anaemia.
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