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Cooperatively folded proteins in random sequence libraries

Nature Structural Biology volume 2, pages 856–864 (1995)Cite this article

Abstract

The structural properties of proteins recovered from random sequence libraries can be used to investigate the relationship between folding and sequence information. Here, we show that helical proteins displaying cooperative thermal denaturation transitions can be easily recovered from a library containing 80-residue proteins predominantly composed of glutamine, leucine, and arginine, with an average hydophobicity level similar to that of natural proteins. The native structure of one of these proteins has a stability and oligomeric form similar to that of many natural proteins but differs in having no slowly exchanging amide hydrogens.

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Author notes

  1. Alan R. Davidson

    Present address: Department of Molecular Genetics and Department of Biochemistry, University of Toronto, Toronto, Ontario, M5S 1A8, Canada

Authors and Affiliations

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

    Alan R. Davidson & Robert T. Sauer

  2. Howard Hughes Medical Institute, Whitehead Institute for Biomedical Research, Department of Biology, Massachusetts Institute of Technology, Nine Cambridge Center, Cambridge, Massachusetts, 02142, USA

    Kevin J. Lumb

Authors
  1. Alan R. Davidson
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  2. Kevin J. Lumb
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  3. Robert T. Sauer
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Davidson, A., Lumb, K. & Sauer, R. Cooperatively folded proteins in random sequence libraries. Nat Struct Mol Biol 2, 856–864 (1995). https://doi.org/10.1038/nsb1095-856

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