α-helix mimicry of a β-turn

Georges Mer, Esther Kellenberger, Jean François Lefèvre

Research output: Contribution to journalArticle

17 Scopus citations

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

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Keywords

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

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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