Abstract
A structure consisting of the polyproline-II or collagen-like helix immediately succeeded by a β-turn is seen in several synthetic peptides and has been suggested to be the conformational requirement for proline hydroxylation in nascent procollagen. Using a simple algorithm for detecting secondary structures, we have analysed crystal structure data on 40 globular proteins and have found eight examples of the collagen-helix + β-turn supersecondary structure in 15 proteins that contain the collagen-like helical segments.
Original language | English (US) |
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Pages (from-to) | 705-709 |
Number of pages | 5 |
Journal | Journal of Molecular Biology |
Volume | 198 |
Issue number | 4 |
DOIs | |
State | Published - Dec 20 1987 |
Externally published | Yes |
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Molecular Biology