A novel supersecondary structure in globular proteins comprising the collagen-like helix and β-turn
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A structure consisting of the polyproline-II or collagen-like helix immediately succeeded by a beta-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 + beta-turn supersecondary structure in 15 proteins that contain the collagen-like helical segments.
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