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• W2029794817 startingPage "573" @default.
• W2029794817 abstract "The addition of HCl, at low ionic strength, to the native state of apomyoglobin, beta-lactamase, and cytochrome c caused these proteins to adopt an essentially fully unfolded conformation in the vicinity of pH 2. However, contrary to expectation, the addition of further acid resulted in refolding to a compact conformation with the properties of a molten globule. The major factor responsible for the refolding is believed to be the binding of the anion, which minimizes the intramolecular charge repulsion that initially brought about the unfolding." @default.
• W2029794817 created "2016-06-24" @default.
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• W2029794817 date "1990-01-01" @default.
• W2029794817 modified "2023-10-16" @default.
• W2029794817 title "Acid-induced folding of proteins." @default.
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• W2029794817 doi "https://doi.org/10.1073/pnas.87.2.573" @default.
• W2029794817 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/53307" @default.
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