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Solvation energy in protein folding and binding

Nature volume 319, pages 199–203 (1986)Cite this article

Abstract

We have developed a method for calculating the stability in water of protein structures, starting from their atomic coordinates. The contribution of each protein atom to the solvation free energy is estimated as the product of the accessibility of the atom to solvent and its atomic solvation parameter. Applications of the method include estimates of the relative stability of different protein conformations, estimates of the free energy of binding of ligands to proteins and atomic-level descriptions of hydrophobicity and amphiphilicity.

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Author notes

  1. Andrew D. McLachlan: MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK

Authors and Affiliations

  1. Molecular Biology Institute and Department of Chemistry and Biochemistry, University of California at Los Angeles, Los Angeles, California, 90024, US

    David Eisenberg & Andrew D. McLachlan

Authors
  1. David Eisenberg
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  2. Andrew D. McLachlan
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Eisenberg, D., McLachlan, A. Solvation energy in protein folding and binding. Nature 319, 199–203 (1986). https://doi.org/10.1038/319199a0

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