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- W1963525631 abstract "Information on protein internal motions is usually obtained through the analysis of atomic mean-square displacements, which are a measure of variability of the atomic positions distribution functions. We report a statistical approach to analyze molecular dynamics data on these displacements that is based on probability distribution functions. Using a technique inspired by the analysis of variance, we compute unbiased, reliable mean-square displacements of the atoms and analyze them statistically. We applied this procedure to characterize protein thermostability by comparing the results for a thermophilic enzyme and a mesophilic homolog. In agreement with previous experimental observations, our analysis suggests that the proteins surface regions can play a role in the different thermal behavior." @default.
- W1963525631 created "2016-06-24" @default.
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- W1963525631 date "2004-05-01" @default.
- W1963525631 modified "2023-10-16" @default.
- W1963525631 title "Atomic Mean-Square Displacements in Proteins by Molecular Dynamics: A Case for Analysis of Variance" @default.
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- W1963525631 doi "https://doi.org/10.1016/s0006-3495(04)74330-1" @default.
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