Journal
EXTREMOPHILES
Volume 13, Issue 1, Pages 11-20Publisher
SPRINGER JAPAN KK
DOI: 10.1007/s00792-008-0192-4
Keywords
Thermophiles; Psychrophiles; Cold-adaptation; Stability; Amino acid frequency; Protein structure
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Funding
- Norwegian functional genomics programe (FUGE)
- Norwegian Cancer Society
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Thermophiles, mesophiles, and psychrophiles have different amino acid frequencies in their proteins, probably because of the way the species adapt to very different temperatures in their environment. In this paper, we analyse how contacts between sidechains vary between homologous proteins from species that are adapted to different temperatures, but displaying relatively high sequence similarity. We investigate whether specific contacts between amino acids sidechains is a key factor in thermostabilisation in proteins. The dataset was divided into two subsets with optimal growth temperatures from 0-40 and 35-102A degrees C. Comparison of homologues was made between low-temperature species and high-temperature species within each subset. We found that unspecific interactions like hydrophobic interactions in the core and solvent interactions and entropic effects at the surface, appear to be more important factors than specific contact types like salt bridges and aromatic clusters.
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