Some thermodynamic implications for the thermostability of proteins

Citation
Dc. Rees et Ad. Robertson, Some thermodynamic implications for the thermostability of proteins, PROTEIN SCI, 10(6), 2001, pp. 1187-1194
Citations number
41
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Biochemistry & Biophysics
Journal title
PROTEIN SCIENCE
ISSN journal
0961-8368 → ACNP
Volume
10
Issue
6
Year of publication
2001
Pages
1187 - 1194
Database
ISI
SICI code
0961-8368(200106)10:6<1187:STIFTT>2.0.ZU;2-Y
Abstract
An analysis of the thermodynamics of protein stability reveals a general te ndency for proteins that denature at higher temperatures to have greater fr ee energies of maximal stability. To a reasonable approximation, the temper ature 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 l east for these proteins, that thermostability tends to be achieved through elevation of the stability curve rather than by broadening or through a hor izontal shift to higher temperatures. The relationship between the free ene rgy of maximal stability and the temperature of heat denaturation is such t hat 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 t he energetic consequences of thermal expansion suggests that these effects may contribute significantly to the destabilization of the native state of proteins with increasing temperature.