A novel supersecondary structure in globular proteins comprising the collagen-like helix and β-turn

V. S. Ananthanarayanan, K. V. Soman, C. Ramakrishnan

Research output: Contribution to journalArticle

9 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)705-709
Number of pages5
JournalJournal of Molecular Biology
Volume198
Issue number4
DOIs
StatePublished - Dec 20 1987
Externally publishedYes

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Collagen
Procollagen
Proteins
Hydroxylation
Proline
Peptides
polyproline

ASJC Scopus subject areas

  • Virology

Cite this

A novel supersecondary structure in globular proteins comprising the collagen-like helix and β-turn. / Ananthanarayanan, V. S.; Soman, K. V.; Ramakrishnan, C.

In: Journal of Molecular Biology, Vol. 198, No. 4, 20.12.1987, p. 705-709.

Research output: Contribution to journalArticle

Ananthanarayanan, V. S. ; Soman, K. V. ; Ramakrishnan, C. / A novel supersecondary structure in globular proteins comprising the collagen-like helix and β-turn. In: Journal of Molecular Biology. 1987 ; Vol. 198, No. 4. pp. 705-709.
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