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• W2041673590 endingPage "R114" @default.
• W2041673590 startingPage "R107" @default.
• W2041673590 abstract "Protein folding is a reaction in which an extended polypeptide chain acquires maximal packing through formation of secondary and tertiary structures. Compactness and shape are, therefore, critical properties characterizing the process of protein folding. Because the stability of the native state is determined by the subtle free energy balance between the native and denatured states, the characterization of the denatured state is also essential to understand the conformational stability of the native state. We show that solution X-ray scattering is the best technique available today to address these problems. Although the structural resolution of the unfolded or compact denatured states elucidated from solution X-ray scattering is low, it provides a variety of information complementary to that obtained by NMR or X-ray crystallography." @default.
• W2041673590 created "2016-06-24" @default.
• W2041673590 creator A5022600763 @default.
• W2041673590 creator A5039096245 @default.
• W2041673590 date "1996-10-01" @default.
• W2041673590 modified "2023-10-13" @default.
• W2041673590 title "X-ray solution scattering studies of protein folding" @default.
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• W2041673590 doi "https://doi.org/10.1016/s1359-0278(96)00047-8" @default.
• W2041673590 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/9080178" @default.
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