THE EXTRA-STABILITY OF THERMOPHILIC GLOBULAR-PROTEINS - A THERMODYNAMIC APPROACH

Citation
G. Graziano et al., THE EXTRA-STABILITY OF THERMOPHILIC GLOBULAR-PROTEINS - A THERMODYNAMIC APPROACH, Thermochimica acta, 269, 1995, pp. 381-392
Citations number
49
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Chemistry Analytical
Journal title
ISSN journal
0040-6031
Volume
269
Year of publication
1995
Pages
381 - 392
Database
ISI
SICI code
0040-6031(1995)269:<381:TEOTG->2.0.ZU;2-D
Abstract
In this paper a general thermodynamic analysis of the Gibbs energy cha nge associated with the two-state denaturation process of small globul ar proteins is presented. The proposed ''parabolic approximation'' to the Gibbs energy change, apart from an analytical relationship for cal culating the hot and cold denaturation temperatures, emphasizes the li miting thermodynamic mechanisms that a globular protein can exploit to increase its thermostability. These mechanisms are critically discuss ed, by stressing the fact that, actually, they are mutually dependent, due to the strong temperature-dependence of denaturation enthalpy and entropy changes.