BIOMOLECULES AND ENZYMES

Detailed explanation-1: -The -helix is very compact. Each full turn has 3.6 amino acid residues, and each amino acid is advanced 1.5 angstrom units (Å) along the helix axis (1 Å = 10–1 nm = 10–4 m = 10–7 mm).

Detailed explanation-2: -Alpha-helices have 3.6 amino acid residues per turn, ie a helix 36 amino acids long would form 10 turns. The separation of residues along the helix axis is 5.4/3.6 or 1.5 Angstroms, ie the alpha-helix has a rise per residue of 1.5 Angstroms.

Detailed explanation-3: -The -helix is also known as 3. 613 helix, since each turn of the helix has approximately 3. 6 amino acid residue and a 13− member ring is formed by hydrogen bonding.

Detailed explanation-4: -The alpha helix is also called a classic Pauling–Corey–Branson -helix. The name 3.613-helix is also used for this type of helix, denoting the average number of residues per helical turn, with 13 atoms being involved in the ring formed by the hydrogen bond.