How random is a highly denatured protein?
Biophys Chem
; 53(1-2): 105-13, 1994 Dec.
Article
em En
| MEDLINE
| ID: mdl-17020841
ABSTRACT
There has been renewed interest in determining the physicochemical properties of denatured states of proteins. In many denatured states there is evidence for the existence of nonrandom configurational distributions. Here we examine the small-angle neutron scattering profile of yeast phosphoglycerate kinase in the native state and in highly denaturing conditions. We show that the denatured protein scattering profile can be interpreted using a model developed for synthetic polymers in which the chain behaves as a random coil in a good solvent, i.e. with excluded volume interactions. The implications of this result for our appreciation of the protein folding process are discussed.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Tipo de estudo:
Clinical_trials
Idioma:
En
Revista:
Biophys Chem
Ano de publicação:
1994
Tipo de documento:
Article
País de afiliação:
França