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- W2080475072 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." @default.
- W2080475072 created "2016-06-24" @default.
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- W2080475072 date "1994-12-01" @default.
- W2080475072 modified "2023-10-14" @default.
- W2080475072 title "How random is a highly denatured protein?" @default.
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- W2080475072 doi "https://doi.org/10.1016/0301-4622(94)00081-6" @default.
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