THE FUNCTION OF VITRIFICATION IN NATIVE S TRUCTURE PRESERVATION IN PROTEIN DEHYDRATION PROCESS

Citation
Iv. Sochava et al., THE FUNCTION OF VITRIFICATION IN NATIVE S TRUCTURE PRESERVATION IN PROTEIN DEHYDRATION PROCESS, Biofizika, 40(1), 1995, pp. 48-53
Citations number
18
Categorie Soggetti
Biophysics
Journal title
ISSN journal
00063029
Volume
40
Issue
1
Year of publication
1995
Pages
48 - 53
Database
ISI
SICI code
0006-3029(1995)40:1<48:TFOVIN>2.0.ZU;2-9
Abstract
Concentration dependencies of maximum temperature (T(d), thermal effec t of denaturation (DELTAQ(d)) and also of glass transition temperature (T(g)) were obtained in heat capacity investigation of five globular proteins with low water content. Special features of the observed T(d) and DELTAQ(d) dependencies, both general for polymers and specific fo r proteins, are discussed. The assumption is put forward that anomalou sly strong dependence of protein T(g) on humidity, bringing together g lass and denaturation transitions, results in the fact that denaturati on process can be observed in completely dehydrated proteins. The dena turation parameters of dry proteins were determined.