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A surprising simplicity to protein folding

Nature volume 405, pages 39–42 (2000)Cite this article

Abstract

The polypeptide chains that make up proteins have thousands of atoms and hence millions of possible inter-atomic interactions. It might be supposed that the resulting complexity would make prediction of protein structure and protein-folding mechanisms nearly impossible. But the fundamental physics underlying folding may be much simpler than this complexity would lead us to expect: folding rates and mechanisms appear to be largely determined by the topology of the native (folded) state, and new methods have shown great promise in predicting protein-folding mechanisms and the three-dimensional structures of proteins.

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Authors and Affiliations

  1. Department of Biochemistry, University of Washington, J567 Health Sciences Building, Box 357350, Seattle, 98195, Washington, USA

    David Baker

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Baker, D. A surprising simplicity to protein folding. Nature 405, 39–42 (2000). https://doi.org/10.1038/35011000

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