Third type of secondary structure: Noncooperative mobile conformation. Protein Data Bank analysis

• Published in: Biochemical and biophysical research communications Vol. 146; no. 3; pp. 934 - 938
• Main Authors: Adzhubei, A.A., Eisenmenger, F., Tumanyan, V.G., Zinke, M., Brodzinski, S., Esipova, N.G.
• Format: Journal Article
• Language: English
• Published: San Diego, CA Elsevier Inc 14.08.1987; Elsevier
• Subjects: Amino Acids; Applied sciences; Exact sciences and technology; Information Systems; Other techniques and industries; Protein Conformation; Proteins; secondary structure
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1016/0006-291X(87)90736-4

Analysis of 68 proteins from Protein Data Bank disclosed a new widely spread type of the secondary structure that is designated as mobile (M-) conformation. Helical parameters of M-conformation are close to the poly-L-proline II type helix. Its occurrence in globular proteins approximates that of the β-sheet. The angles corresponding to the position of the M-conformation maximum in distribution of amino acid residues on a conformational map are ϕ: −65°, ψ: 140°. Unique features and high occurrence in proteins make it possible to distinguish the M-conformation as an independent third type of the secondary structure in globular proteins, that should be included in the present classification.