期刊
PROTEIN SCIENCE
卷 16, 期 9, 页码 1887-1895出版社
WILEY
DOI: 10.1110/ps.072947007
关键词
protein stability; protein folding; temperature dependence; hydrophobic effect; salt bridges
资金
- Medical Research Council [MC_U117573805] Funding Source: Medline
- MRC [MC_U117573805] Funding Source: UKRI
- Medical Research Council [MC_U117573805] Funding Source: researchfish
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.
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