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- W1997334690 abstract "The conformational stability of gamma-II crystallin at pH 7.0 was estimated by studying its urea denaturation at isothermal conditions. The conformational states were monitored by far UV-CD and fluorescence measurements. Gamma-II crystallin shows sigmoidal order—disorder transition curves by both methods. The presence of more than one intermediate was confirmed but at neutral pH. The experiment results were critically analyzed in terms of both linear extrapolation and Tanford's models. The Gibbs free energy of unfolding ΔGu,H2O = − 36 kcal mol−1 was obtained. This value corresponds to the high conformational stability of the protein predicted qualitatively by its crystal structure." @default.
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- W1997334690 date "1993-12-01" @default.
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- W1997334690 title "Urea unfolding and stability of gamma-II crystallin" @default.
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- W1997334690 doi "https://doi.org/10.1016/1011-1344(93)80181-8" @default.
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