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Nat Struct Biol. 1994 Sep;1(9):584-90.

A short linear peptide that folds into a native stable beta-hairpin in aqueous solution.

Author information

1
European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.

Abstract

The conformational properties of a 16 residue peptide, corresponding to the second beta-hairpin of the B1 domain of protein G, have been studied by nuclear magnetic resonance spectroscopy (NMR). This fragment is monomeric under our experimental conditions and in pure water adopts a population containing up to 40% native-like beta-hairpin structure. The detection by NMR of a native-like beta-hairpin in aqueous solution, reported here for the first time, indicates that these structural elements may have an important role in the early steps of protein folding. It also provides a good model to study in detail the sequence determinants of beta-hairpin structure stability, as has been done with alpha-helices.

PMID:
7634098
DOI:
10.1038/nsb0994-584
[Indexed for MEDLINE]

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