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

被引：7

作者：

CALMETTES, P

DURAND, D

RECEVEUR, V

DESMADRIL, M

MINARD, P

DOUILLARD, R

机构：

[1] UNIV PARIS 11,ENZYMOL PHYSICOCHIM & MOLEC LAB,CNRS,F-91405 ORSAY,FRANCE

[2] INRA,BIOCHIM & TECHNOL PROT LAB,F-44026 NANTES 03,FRANCE

来源：

PHYSICA B | 1995年 / 213卷

关键词：

D O I：

10.1016/0921-4526(95)00270-J

中图分类号：

O469 [凝聚态物理学];

学科分类号：

070205 ;

摘要：

Small-angle neutron-scattering profiles from denatured yeast phosphoglycerate 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 random 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.

引用

页码：754 / 756

页数：3

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