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Mutational analysis of a protein-folding pathway

Nature volume 338, pages 127–132 (1989)Cite this article

Abstract

The effects of amino-acid replacements on the disulphide-coupled folding pathway of bovine pancreatic trypsin inhibitor have been examined. Replacements at three sites destabilize the native protein relative to the unfolded state, but have different effects on the relative stabilities of the disulphide-bonded folding intermediates, thus allowing the roles of the altered residues during folding to be distinguished.

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Authors and Affiliations

  1. Department of Biology, University of Utah, Salt Lake City, Utah, 84112, USA

    David P. Goldenberg, Richard W. Frieden, Julie A. Haack & Thomas B. Morrison

Authors
  1. David P. Goldenberg
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  2. Richard W. Frieden
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  3. Julie A. Haack
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  4. Thomas B. Morrison
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Goldenberg, D., Frieden, R., Haack, J. et al. Mutational analysis of a protein-folding pathway. Nature 338, 127–132 (1989). https://doi.org/10.1038/338127a0

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