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A peptide model of a protein folding intermediate

Nature volume 336, pages 42–48 (1988)Cite this article

Abstract

It is difficult to determine the structures of protein folding intermediates because folding is a highly cooperative process. A disulphide-bonded peptide pair, designed to mimic the first crucial intermediate in the folding of bovine pancreatic trypsin inhibitor, contains secondary and tertiary structure similar to that found in the native protein. Peptide models like this circumvent the problem of cooperativity and permit characterization of structures of folding intermediates.

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Authors and Affiliations

  1. Whitehead Institute for Biomedical Research, Nine Cambridge Center, Cambridge, Massachusetts, 02142, USA

    Terrence G. Oas

  2. Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts, 02139, USA

    Peter S. Kim

Authors
  1. Terrence G. Oas
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  2. Peter S. Kim
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Oas, T., Kim, P. A peptide model of a protein folding intermediate. Nature 336, 42–48 (1988). https://doi.org/10.1038/336042a0

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