BIOMOLECULES AND ENZYMES

Detailed explanation-1: -The most common types of secondary structures are the helix and the pleated sheet. Both structures are held in shape by hydrogen bonds, which form between the carbonyl O of one amino acid and the amino H of another. Images showing hydrogen bonding patterns in beta pleated sheets and alpha helices.

Detailed explanation-2: -Primarily, the interactions among R groups creates the complex three-dimensional tertiary structure of a protein. The nature of the R groups found in the amino acids involved can counteract the formation of the hydrogen bonds described for standard secondary structures such as the alpha helix.

Detailed explanation-3: -The tertiary structure is the overall shape of the polypeptide that results from interactions and hydrogen bonding between the side chains, or R groups, of the various amino acids present. It is during this stage of protein formation that disulfide bridges and hydrophobic interactions are first seen.

Detailed explanation-4: -Secondary structure refers to regular, local structure of the protein backbone, stabilised by intramolecular and sometimes intermolecular hydrogen bonding of amide groups.

Detailed explanation-5: -The R groups (the variant groups) of the polypeptide protrude out from the -helix chain. In the -pleated sheet, the “pleats” are formed by hydrogen bonding between atoms on the backbone of the polypeptide chain. The R groups are attached to the carbons and extend above and below the folds of the pleat.