University:
Liberty University
Course:
BIOM 500 | Introduction to Biomedical Sciences
Academic year:

2024
Views:

201

Pages:

5
Author:

Sheha A.

Alpha Helix This is the most common secondary structure found in proteins. α-helix seen in hemoglobin, myoglobin, collagen, etc. α-helix is a right-handed coiled structure. α-helix structure is stabilized by hydrogen bonds. Extensive hydrogen bonding between the peptide bonds. C=O group of 6th amino acid is hydrogen bonded with the N-H group of 9th amino acid. The hydrogen bonds are parallel to the α-helix axis. Hydrogen bonds are individually weak, but collectively large numbers of hydrogen bonds can stabilize the helical structures in stable form. Each turn of helix contains 3.6 amino acid residues and each amino acid is separated by a distance of 1.5A. Proline, glycine, alanine, serine are considered as helix destabilizing amino acids as they disrupt the formation of alpha helix. Amino acid alanine facilitates the helix formation and stabilizes the helix formation.