Journal
PROTEIN SCIENCE
Volume 10, Issue 6, Pages 1187-1194Publisher
WILEY
DOI: 10.1110/ps.180101
Keywords
protein stability; thermal expansion; protein volumes; stability curve
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Funding
- NIGMS NIH HHS [R01 GM045162, R01 GM046869, R37 GM045162, GM45162, GM46869] Funding Source: Medline
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An analysis of the thermodynamics of protein stability reveals a general tendency for proteins that denature at higher temperatures to have greater free energies of maximal stability. To a reasonable approximation, the temperature of maximal stability for the set of globular, water-soluble proteins surveyed by Robertson and Murphy occurs at T* similar to 283K, independent of the heat denaturation temperature, T-m. This observation indicates, at least for these proteins, that thermostability tends to be achieved through elevation of the stability curve rather than by broadening or through a horizontal shift to higher temperatures. The relationship between the free energy of maximal stability and the temperature of heat denaturation is such that an increase in maximal stability of similar to0.008 kJ/mole/residue is, on average, associated with a 1 degreesC increase in T-m. An estimate of the energetic consequences of thermal expansion suggests that these effects may contribute significantly to the destabilization of the native state of proteins with increasing temperature.
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