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.
Atomic mean-square displacements in proteins by molecular dynamics: A case for analysis of variance / Maragliano, L; Cottone, G; Cordone, L; Ciccotti, Giovanni. - In: BIOPHYSICAL JOURNAL. - ISSN 0006-3495. - 86:(2004), pp. 2765-2772. [10.1016/S0006-3495(04)74330-1]
Atomic mean-square displacements in proteins by molecular dynamics: A case for analysis of variance
CICCOTTI, Giovanni
2004
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.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.