Third type of secondary structure: Noncooperative mobile conformation. Protein Data Bank analysis
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 th...
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Published in | Biochemical and biophysical research communications Vol. 146; no. 3; pp. 934 - 938 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
San Diego, CA
Elsevier Inc
14.08.1987
Elsevier |
Subjects | |
Online Access | Get full text |
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Summary: | 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. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0006-291X 1090-2104 |
DOI: | 10.1016/0006-291X(87)90736-4 |