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• W2110222046 abstract "Abstract RNase hydrogen exchange kinetics are similar to the characteristically complex hydrogen exchange of proteins in general. We have analyzed these kinetic data in terms of distributions of first order rates. Two classes of exchanging sites in tritiated RNase can be identified and isolated by their temperature dependence. The pH and cosolvent effects on each class have been measured separately. Each class contains a distribution of first order rates evenly distributed over the range. The rank order of exchange is pH and temperature independent. One class exchanges with an apparent activation energy (E*app) similar to that of random conformation polypeptides and substituted amides, ≃22 kcal. The second class exchanges with an E*app of ≃60 kcal. The number of sites exchanging in each class is pH dependent. At pH 3.15 about 50% of the measured sites exchange with low E*app, while at pH 6 about 90% exchange with low E*app. To account for the range and temperature dependence of the high E*app distribution of exchange rates we propose a model involving an equilibrium between the folded and thermally unfolded state. This model is supported by (a) the agreement between observed and calculated rates estimated from the literature values of the thermal unfolding equilibrium constant, (b) the pH dependence of the high E*app exchange, and (c) the urea and ethanol dependence of the high E*app exchange. It is proposed that the low E*app exchange is from the folded protein, and as such offers a uniquely sensitive probe of the conformational dynamics of the folded state. The pH dependence of the low E*app rates is less than one-third that observed in model random conformational polypeptides." @default.
• W2110222046 created "2016-06-24" @default.
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• W2110222046 date "1971-07-01" @default.
• W2110222046 modified "2023-10-18" @default.
• W2110222046 title "Studies of Hydrogen Exchange in Proteins" @default.
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• W2110222046 doi "https://doi.org/10.1016/s0021-9258(18)62060-5" @default.
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