α-helix mimicry of a β-turn

Georges Mer, Esther Kellenberger, J. F. Lefèvre

Research output: Contribution to journalArticle

17 Citations (Scopus)

Abstract

It is shown here that the three-dimensional arrangement of the amino acids in an RGDF β-turn (sequence involved in cell adhesion) resembles that of an α-helix with a shuffled RGDF sequence (i.e. RGXFD). A mini-protein was designed and constructed which arranges the RGXFD sequence into a well defined helical conformation. The designed protein is bioactive and folds into the desired structure as assessed by nuclear magnetic resonance spectroscopy. The recognition process mediated by a β-turn can thus be mimicked by an α-helix.

Original languageEnglish (US)
Pages (from-to)235-240
Number of pages6
JournalJournal of Molecular Biology
Volume281
Issue number2
DOIs
StatePublished - Aug 14 1998
Externally publishedYes

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Cell Adhesion
Proteins
Magnetic Resonance Spectroscopy
Amino Acids

Keywords

  • α-helix
  • β-turn
  • NMR spectroscopy
  • Protein design
  • Protein folding

ASJC Scopus subject areas

  • Virology

Cite this

α-helix mimicry of a β-turn. / Mer, Georges; Kellenberger, Esther; Lefèvre, J. F.

In: Journal of Molecular Biology, Vol. 281, No. 2, 14.08.1998, p. 235-240.

Research output: Contribution to journalArticle

Mer, G, Kellenberger, E & Lefèvre, JF 1998, 'α-helix mimicry of a β-turn', Journal of Molecular Biology, vol. 281, no. 2, pp. 235-240. https://doi.org/10.1006/jmbi.1998.1939
Mer, Georges ; Kellenberger, Esther ; Lefèvre, J. F. / α-helix mimicry of a β-turn. In: Journal of Molecular Biology. 1998 ; Vol. 281, No. 2. pp. 235-240.
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