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Protein Science (2007), 16:1887-1895. Published by Cold Spring Harbor Laboratory Press. Copyright © 2007 The Protein Society
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Amino-acid interactions in psychrophiles, mesophiles, thermophiles, and hyperthermophiles: Insights from the quasi-chemical approximation

Richard A. Goldstein

Mathematical Biology, National Institute of Medical Research, Mill Hill, London NW7 1AA, United Kingdom

(RECEIVED April 13, 2007; FINAL REVISION June 19, 2007; ACCEPTED June 19, 2007)

We investigate the mechanisms used by proteins to maintain thermostability throughout a wide range of temperatures. We use the quasi-chemical approximation to estimate interaction strengths for psychrophiles, mesophiles, thermophiles, and hyperthermophiles. Our results highlight the importance of core packing in thermophilic stability. Although we observed an increase in the number of charged residues, the contribution of salt bridges appears to be relatively modest by comparison. We observed results consistent with a gradual loosening of structure in psychrophiles, including a weakening of almost all types of interactions.

Keywords: protein stability; protein folding; temperature dependence; hydrophobic effect; salt bridges


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