Repulsive interparticle interactions in a denatured protein solution revealed by small angle neutron scattering.
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.
Receveur
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Laboratoire Léon Brillouin, C.E.A. de Saclay, Gif-sur-Yvette, France. receveur@bioch.ox.ac.uk
Durand
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Desmadril
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Calmettes
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D005656:Fungal Proteins; D009502:Neutrons; D010735:Phosphoglycerate Kinase; D011489:Protein Denaturation; D011506:Proteins / Q000737:chemistry*; D011994:Recombinant Proteins; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D012542:Scattering, Radiation
D005656:Fungal Proteins; D011506:Proteins; D011994:Recombinant Proteins; D010735:Phosphoglycerate Kinase