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• W2024698943 endingPage "320" @default.
• W2024698943 startingPage "313" @default.
• W2024698943 abstract "Reversible GuHCl denaturation of human stefin A (25°C, pH 8) was monitored by the tyrosine fluorescence, by circular dichroism in the near UV and by circular dichroism in the far UV. In each case a midpoint of 2.8 ± 0.1M GuHCl was obtained, demonstrating the cooperativity of the denaturation. Kinetics of the slow folding on diluting the protein from the GuHCl denatured state, was also measured by the three spectroscopic probes (10°C, pH 8). Results conform to a sequential mechanism. Denaturant concentration and temperature dependence of the slow folding were measured by fluorescence. From a linear Arrhenius plot the Eaof100 ± 5kJ/mol was read. ‘Double mixing’ experiments revealed a slow reaction going on in the unfolded state which influenced the amplitude of the fluorescence changes. ‘Double mixing’ experiments performed by FPLC have shown that the folding itself, i.e., the formation of a compact state, was not dependent on the time spent under unfolding conditions." @default.
• W2024698943 created "2016-06-24" @default.
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• W2024698943 date "1991-07-01" @default.
• W2024698943 modified "2023-10-16" @default.
• W2024698943 title "Folding studies of the cysteine proteinase inhibitor — human stefin A" @default.
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• W2024698943 doi "https://doi.org/10.1016/0167-4838(91)90149-t" @default.
• W2024698943 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/1859820" @default.
• W2024698943 hasPublicationYear "1991" @default.
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