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• W2912144168 abstract "The thermal unfolding of ribonuclease at a number of pH values has been studied by 1H nuclear magnetic resonance spectroscopy, under conditions where the unfolding is fully reversible and concentration-independent. At pH∗ 5.5 (uncorrected for the deuterium isotope effect) there is evidence for a conformational change affecting His-48 and perhaps a methionine residue at temperatures below the major thermal transition. No evidence for intermediates in the major transition was found. The product of thermal unfolding under these conditions is not a random coil, and the remaining elements of structure probably include a phenylalanine and two histidine residues. At pH∗ 1.5 and pH∗ 2.9, the product of thermal unfolding is closer to a random coil, and under these conditions the changes in area of the histidine C(2)H resonances with temperature give evidence for the existence of an intermediate in the unfolding process in which His-12 and His-119 are in a solvent-like environment, while His-48 and His-105 are not (see Westmoreland & Matthews (1973)). The changes in the spectra of ribonuelease between pH∗ 5.5 and pH∗ 1.5 are described, and the possible relation between these changes and the alterations in thermal unfolding with pH are discussed." @default.
• W2912144168 created "2019-02-21" @default.
• W2912144168 creator A5045237764 @default.
• W2912144168 creator A5045559341 @default.
• W2912144168 date "1975-01-01" @default.
• W2912144168 modified "2023-09-26" @default.
• W2912144168 title "Nuclear magnetic resonance studies of the unfolding of pancreatic ribonuclease" @default.
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• W2912144168 doi "https://doi.org/10.1016/0022-2836(75)90385-x" @default.
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