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Metastable states and folding free energy barriers

Nature Structural Biology volume 5, pages 1021–1024 (1998)Cite this article

Abstract

The demonstration that the native state of a long lived protease is less stable than a partially folded 'molten globule' like state shatters long standing preconceptions about protein folding.

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Figure 1: Pro region–protease complexes of a, α-lytic protease and b, subtilisin.
Figure 2: Structures of pro regions of a, carboxypeptidase A, b , subtilisin, and c, α-lytic protease (C-terminal domain).

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Acknowledgements

I thank A. Murzin for helpful discussions of the structural similarities among the pro regions, J. Tsai for help with the figures and D. Agard's group for comments on the manuscript.

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Authors and Affiliations

  1. the Department of Biochemistry at the University of Washington, Seattle, 98195, Washington, USA

    David Baker

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  1. David Baker
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Baker, D. Metastable states and folding free energy barriers. Nat Struct Mol Biol 5, 1021–1024 (1998). https://doi.org/10.1038/4130

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