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60- College Biochemistry - V The a-amino acids polymerize, at least conceptually through the elimination of a water molecule. The resulting (- CO - NH) linkage is known as "peptide bond". Polymers composed of two, three, a few (3 - 10) and many amino acid residues (alternatively called peptide units) are known as Dipeptides, tripeptides, oligopeptides and polypeptides respecti vely. R R I I H2N - CH - coloH + HIHN - CH - COOH _-_H..... z°---7) ex - Amino acid ex - Amino acid R~R I II I C-NH CH-COOH H2N-CH Peptide bond Polypeptide When many acids are joined together by peptide bonds are called polypeptide.
B) Maltose (c) Cellobiose (a) Sucrose (cane sugar) (d) Isomaltose 35. Point out the main difference between reducing and non-reducing sugar. 36. Sucrose is non-reducing sugar. Why? 37. Isomaltose is a reducing sugar. Why? 38. Trehalose is a non-reducing sugar why? Write the structure of it and mention the linkage. 39. What are the biological importance of isomaltose and trehalose. 40. What are polysaccharides? Give an example. 41. What are homo and heteropolysaccharides? Give one example to each.
3. 4. 64 5. 88 6. Alanine 7. 8. 59 Zwitter Ion in Amino Acids In an aqueous solution the amino acids exist as a charged molecules. This is because they contain both an acidic -COOH group which is a proton donor and a basic -NH2 group which is a proton acceptor. Thus the amino acids form a dipolar ion called Zwitter-ion. This zwitter ion is in equilibrium with covalent form of the amino acid. o o R -CH -~ -tH JJ II R -CH -C -0- a - Amino acid I @NH 3 Zwitter ion A Zwitter ion is an amino acid molecule containing both the types of charges is positive and negative charge.