Information on protein internal motions is usually obtained through the analysis of atomic mean-squaredisplacements, which are a measure of variability of the atomic positions distribution functions. We report a statistical approach toanalyze molecular dynamics data on these displacements that is based on probability distribution functions. Using a techniqueinspired by the analysis of variance, we compute unbiased, reliable mean-square displacements of the atoms and analyze themstatistically. We applied this procedure to characterize protein thermostability by comparing the results for a thermophilic enzymeand a mesophilic homolog. In agreement with previous experimental observations, our analysis suggests that the proteinssurface regions can play a role in the different thermal behavior.
|Numero di pagine||1|
|Stato di pubblicazione||Published - 2004|