STRUCTURES OF PHOSPHOGLYCERATE KINASE AND BETA-CASEIN DENATURED IN GUANIDINIUM CHLORIDE

Authors
CALMETTES P DURAND D RECEVEUR V DESMADRIL M MINARD P DOUILLARD R
Citation
P. Calmettes et al., STRUCTURES OF PHOSPHOGLYCERATE KINASE AND BETA-CASEIN DENATURED IN GUANIDINIUM CHLORIDE, Physica. B, Condensed matter, 213, 1995, pp. 754-756
Citations number
8
Categorie Soggetti
Physics, Condensed Matter
Journal title
Physica. B, Condensed matter → ACNP
ISSN journal
09214526
Volume
213
Year of publication
1995
Pages
754 - 756
Database
ISI
SICI code
0921-4526(1995)213:<754:SOPKAB>2.0.ZU;2-D
Abstract
Small-angle neutron-scattering profiles from denatured yeast phosphogl ycerate kinase (PGK) and beta-casein are presented. The denaturant was deuterated guanidinium chloride (Gdn-HCl) in heavy water. In about 4 M Gdn-HCl these two very different proteins were found to behave as ra ndom coils with excluded-volume interactions. This means that they are highly or totally unfolded. At denaturant concentrations between 0.4 and 1.1 M, intermediate structural states were observed for PGK whose radius of gyration varies from about 23 to 71 Angstrom.