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- W2060833904 abstract "Protein dynamics is crucial for protein function. Proteins in living systems are not isolated, but operate in networks and in a carefully regulated environment. Understanding the external control of protein dynamics is consequently important. Hydration and solvent viscosity are among the salient properties of the environment. Dehydrated proteins and proteins in a rigid environment do not function properly. It is consequently important to understand the effect of hydration and solvent viscosity in detail. We discuss experiments that separate the two effects. These experiments have predominantly been performed with wild-type horse and sperm whale myoglobin, using the binding of carbon monoxide over a broad range of temperatures as a tool. The experiments demonstrate that data taken only in the physiological temperature range are not sufficient to understand the effect of hydration and solvent on protein relaxation and function. While the actual data come from myoglobin, it is expected that the results apply to most or all globular proteins." @default.
- W2060833904 created "2016-06-24" @default.
- W2060833904 creator A5023078378 @default.
- W2060833904 creator A5047461991 @default.
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- W2060833904 date "2002-07-01" @default.
- W2060833904 modified "2023-10-16" @default.
- W2060833904 title "Hydration, slaving and protein function" @default.
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- W2060833904 doi "https://doi.org/10.1016/s0301-4622(02)00083-2" @default.
- W2060833904 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/12128188" @default.
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