BIOMOLECULES AND ENZYMES

Detailed explanation-1: -The-helix is maintained by hydrogen bonds between the peptide bonds. Each peptide bond C-O is hydrogen bonded to the peptide bond N-H four amino acid residues ahead of it. Each C-O and each N-H in the main chain are hydrogen bonded.

Detailed explanation-2: -Hydrogen bonding between amino groups and carboxyl groups in neighboring regions of the protein chain sometimes causes certain patterns of folding to occur. Known as alpha helices and beta sheets, these stable folding patterns make up the secondary structure of a protein.

Detailed explanation-3: -Each -helix contains three H-bonding chains of five amide hydrogen bonds (illustrated in Figure 2) except for the polyalanine isomer II, which has only 14 “normal” H-bonds. In addition, a terminal H-bonding C O interacts with a second N H to form an H-bond to an additional amide (see Figure 1).

Detailed explanation-4: -Answer: A are roughly perpendicular to the axis of the helix. C) occur mainly between electronegative atoms of the R groups. D) occur only between some of the amino acids of the helix.

Detailed explanation-5: -In the -helix in its canonical Pauling form, all hydrogen bonds were formed by intramolecular interactions.