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- W2066415535 abstract "The rates of protein conformational changes are usually not only limited by external but also internal friction, however, the origin and significance of this latter phenomenon is poorly understood. It is often found experimentally that a linear fit to the reciprocal of the reaction rate as a function of the viscosity of the external medium has a non-zero value at zero viscosity, signifying the presence of internal friction. To better understand this phenomenon, we have performed molecular dynamics simulations of a conformation change of trypsin, where we could separately control the friction of the surface and the interior of the protein. Here we present the results of our simulations, and also compare them to the experimental data obtained for the activation of trypsin." @default.
- W2066415535 created "2016-06-24" @default.
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- W2066415535 date "2013-01-01" @default.
- W2066415535 modified "2023-09-29" @default.
- W2066415535 title "The Internal Friction of Proteins Determined by MD Simulations" @default.
- W2066415535 doi "https://doi.org/10.1016/j.bpj.2012.11.360" @default.
- W2066415535 hasPublicationYear "2013" @default.
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