Topological Properties of Chemical Bonds from Static and Dynamic Electron Densities.

ABSTRACT: Dynamic and static electron densities (EDs) based on the independent spherical atom model (IAM) and multipole (MP) models of crambin were successfully computed, holding no series-termination effects. The densities are compared to EDs of small biological molecules at diverse temperatures. It is outlined that proteins exhibit an intrinsic flexibility, present as frozen disorder at 100 K, in contrast to small molecules. The flexibility of the proteins is reflected by atomic displacement parameters (B-factors), which are considerably larger than for small molecules at 298 K. Thus, an optimal deconvolution of deformation density and thermal motion is not guaranteed, which prevents a free refinement of MP parameters but allows an application of transferable, fixed MP parameters. The analysis of

SUBMITTER: Jagannatha Prathapa S 

PROVIDER: S-EPMC4431502 | biostudies-literature | 2013 Sep

REPOSITORIES: biostudies-literature