Repulsive interparticle interactions in a denatured protein solution revealed by small angle neutron scattering

FEBS Letters

Desmadril, Michel¹  Receveur, Véronique²  Calmettes, Patrick²  Durand, Dominique² 

[1] Laboratoire de Modélisation et d'Ingénierie des Protéines, Université de Paris-Sud, 91405 Orsay cedex, France;Laboratoire Léon Brillouin, C.E.A. de Saclay, 91191 Gif-sur-Yvette cedex, France

关键词: Denatured state of protein interactions;    Interparticle;    Second virial coefficient;    Small angle neutron scattering;    Phosphoglycerate kinase;    SANS;    small angle neutron scattering;    SAXS;    small angle X-ray scattering;    SAS;    small angle scattering;    PGK;    yeast phosphoglycerate kinase;    Gdm-Cl;    guanidinium chloride;   

DOI  :  10.1016/S0014-5793(98)00309-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

In order to investigate the effect of concentration in biological processes such as protein folding, small angle neutron scattering measurements were used to determine the second virial coefficient of solutions of both native and strongly denatured phosphoglycerate kinase and the radius of gyration of the protein at zero concentration. The value of the second virial coefficient is a good probe of the non-ideality of a solution. The present results show that the unfolding of the protein leads to a drastic change in the repulsive intermolecular interactions. We conclude that these interactions are due mainly to the behaviour of the denatured polypeptide chain as an excluded volume polymer.

【 授权许可】

Unknown