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

Nature Structural Biology volume 1, pages 584–590 (1994)Cite this article

Abstract

The conformational properties of a 16 residue peptide, corresponding to the second β-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 β-hairpin structure. The detection by NMR of a native-like β-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 β-hairpin structure stability, as has been done with α-helices.

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Authors and Affiliations

  1. European Molecular Biology Laboratory (EMBL), Postfach 102209, Meyerhofstrasse 1, 69012, Heidelberg, Germany

    Francisco J. Blanco & Luis Serrano

  2. Centro de Investigaciones Biológicas, CSIC, Velázquez 144, 28006, Madrid, Spain

    Germán Rivas

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  1. Francisco J. Blanco
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  3. Luis Serrano
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Blanco, F., Rivas, G. & Serrano, L. A short linear peptide that folds into a native stable β-hairpin in aqueous solution. Nat Struct Mol Biol 1, 584–590 (1994). https://doi.org/10.1038/nsb0994-584

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