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• W2041504673 abstract "In this paper, we present an analysis of the soluble species formed on refolding of RNase A at various concentrations, in order to characterize these species with respect to structure and activities. Studies were carried out using reverse-phase high-performance liquid chromatography, circular dichroism, chromatography and ultracentrifugation. At all concentrations of protein used, RNase A refolded to the native form, together with formation of non-native species. These non-native species are either misfolded monomers or aggregates; the percentage of such species increases with increasing concentration of enzyme. Such aggregation appears to be a non-random process governed by intermolecular disulfide crosslinking between monomers. These results reaffirm the principle that the information for folding of the protein is encoded in the amino acid sequence itself." @default.
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• W2041504673 date "1994-01-01" @default.
• W2041504673 modified "2023-09-25" @default.
• W2041504673 title "Refolding of RNase A at high concentrations: identification of non-native species" @default.
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• W2041504673 doi "https://doi.org/10.1016/0141-8130(94)90047-7" @default.
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