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ArticlesCopyright © 1990 by American Association for the Advancement of Science
Inclusion of thermal motion in crystallographic structures by restrained molecular dynamics
BIOSON Research Institute, University of Groningen, The Netherlands.
A protein crystal structure is usually described by one single structure, which largely omits the dynamical behavior of the molecule. A molecular dynamics method with a time-averaged crystallographic restraint was used to overcome this limitation. This method yields an ensemble of structures in which all possible thermal motions are allowed, that is, in additional to isotropic distributions, anisotropic and anharmonic positional distributions occur as well. In the case of bovine pancreatic phospholipase A2, this description markedly improves agreement with the observed x-ray diffraction data compared to the results of the classical one-model structure description. Time-averaged crystallographically restrained molecular dynamics reveals large mobilities in the loops involved in lipid bilayer association.
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Science. ISSN 0036-8075 (print), 1095-9203 (online)
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