Quantified electrostatic preorganization in enzymes using the geometry of the electron charge density.

ABSTRACT: Electrostatic preorganization is thought to be a principle factor responsible for the impressive catalytic capabilities of enzymes. The full protein structure is believed to facilitate catalysis by exerting a highly specific electrostatic field on the active site. Computationally determining the extent of electrostatic preorganization is a challenging process. We propose using the topology and geometry of the electron charge density in the enzyme's active site to asses the effects of electrostatic preorganization. In support of this approach we study the convergence of features of the charge density as the size of the active site model increases in Histone Deacetylase 8. The magnitude of charge density at critical points and most Bader atomic charges are found to converge quickly as more o

SUBMITTER: Morgenstern A 

PROVIDER: S-EPMC5612031 | biostudies-literature | 2017 Jul

REPOSITORIES: biostudies-literature