BIOMOLECULES AND ENZYMES

Detailed explanation-1: --Helices, -sheets, and triple helices are three types of secondary structures. All are formed and stabilized by noncovalent interactions, mainly hydrogen bonds.

Detailed explanation-2: -Hydrogen bonds are stabilizing an alpha-helix. The alpha-helix (-helix) is a common motif in the secondary structure of proteins and is a right hand-coiled or spiral conformation (helix) in which every backbone N−H group donates a hydrogen bond to the backbone C=O. group of the amino acid.

Detailed explanation-3: -Two major factors stabilize the alpha helix: intrachain H-bonding and minimization of steric interference between side chains. H-bonds (colored green here) form between the oxygen of one peptide bond and the amide hydrogen four amino acids away from it along the helix.

Detailed explanation-4: -The insulin molecule consists of two peptide chains, the A-chain and the B-chain, linked by two disulfide bonds.

Detailed explanation-5: -Protein -sheet structures are formed by the lateral alignment of -strands in parallel or antiparallel orientations and are stabilized by hydrogen bonding, hydrophobic interactions, and other forces (Figure 1).