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- W1519147602 abstract "The pH dependence and the temperature dependence of the nuclear magnetic resonance spectrum of horse ferrocytochrome c are described. This protein is very stable; it maintains an ordered structure over the pH range 4 to 12 at 25 °C and over the temperature range 4°C to 97 °C at pH 7.0. The dynamic characteristics of the conformation of ferrocytochrome c were investigated. Particular emphasis was laid on the aromatic resonances and resonances of methyl groups shifted far upheld. Tyr‐48 and Phe‐46 were found to be relatively immobile whilst a region of the protein close to Ile‐57 was found to be relatively flexible." @default.
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- W1519147602 date "1980-02-01" @default.
- W1519147602 modified "2023-10-15" @default.
- W1519147602 title "Nuclear-Magnetic-Resonance Studies of Ferrocytochrome c. pH and Temperature Dependence" @default.
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- W1519147602 doi "https://doi.org/10.1111/j.1432-1033.1980.tb05975.x" @default.
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