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Some thermodynamic implications for the thermostability of proteins
Author(s) -
Rees Douglas C.,
Robertson Andrew D.
Publication year - 2001
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.180101
Subject(s) - thermostability , globular protein , thermodynamics , chemistry , denaturation (fissile materials) , heat capacity , protein stability , thermal stability , stability (learning theory) , crystallography , biochemistry , physics , enzyme , organic chemistry , nuclear chemistry , machine learning , computer science
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* ∼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 ∼0.008 kJ/mole/residue is, on average, associated with a 1°C 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.