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- W2066917170 abstract "Molecular dynamics simulation has been performed on five native proteins in water to evaluate their intrinsic isothermal compressibilities βT,int. To identify physical factors contributing to protein compressibility, a general method is presented for analyzing the compressibility of mechanically inhomogeneous systems. The value of βT,int varies with protein species considerably: β-lactoglobulin (14.15×10−2GPa−1) is more than twice as compressible as ribonuclease A (6.77×10−2GPa−1). β-lactoglobulin and myoglobin (13.95×10−2GPa−1) have similar values of βT,int, but the mechanisms responsible for them are significantly different. The volume fluctuations of internal cavities and the magnitudes of the crosscorrelation between them are the key factors determining βT,int of proteins. Though the volume fractions of internal cavity for the five studied proteins are nearly equal to one another, the mean cavity compressibilities βT,cav vary considerably with protein species and range from 0.35to0.69GPa−1, which are much smaller than those of normal organic liquids such as methanol, ethanol, and benzene and close to that of glycerol (0.55GPa−1), a strongly associated liquid." @default.
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- W2066917170 date "2006-08-01" @default.
- W2066917170 modified "2023-09-27" @default.
- W2066917170 title "Evaluation of intrinsic compressibility of proteins by molecular dynamics simulation" @default.
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- W2066917170 doi "https://doi.org/10.1063/1.2219741" @default.
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