THE TEMPERATURE-INDUCED DENATURATION OF SMALL GLOBULAR-PROTEINS AS A FIRST-ORDER PHASE-TRANSITION OF CRYSTAL MOLECULES

Citation
G. Graziano et al., THE TEMPERATURE-INDUCED DENATURATION OF SMALL GLOBULAR-PROTEINS AS A FIRST-ORDER PHASE-TRANSITION OF CRYSTAL MOLECULES, Journal of thermal analysis, 44(4), 1995, pp. 765-775
Citations number
51
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Chemistry Analytical
Journal title
ISSN journal
0368-4466
Volume
44
Issue
4
Year of publication
1995
Pages
765 - 775
Database
ISI
SICI code
0368-4466(1995)44:4<765:TTDOSG>2.0.ZU;2-E
Abstract
A general feature of temperature-induced reversible denaturation of sm all globular proteins is its all-or-none character. This strong cooper ativity leads to think that protein molecules, possessing only two acc essible thermodynamic states, the native and the denatured one, resemb le 'crystal molecules' that melt at raising temperature. An analysis, grounded on mean field theory, allows to conclude that the two-state t ransition is a first-order phase transition. The implication of this c onclusion are briefly discussed.