A quantitative measure of electrostatic perturbation in holo and apo enzymes induced by structural changes.

ABSTRACT: Biological pathways are subject to subtle manipulations that achieve a wide range of functional variation in differing physiological niches. In many instances, changes in the structure of an enzyme on ligand binding germinate electrostatic perturbations that form the basis of its changed catalytic or transcriptional efficiency. Computational methods that seek to gain insights into the electrostatic changes in enzymes require expertise to setup and computing prowess. In the current work, we present a fast, easy and reliable methodology to compute electrostatic perturbations induced by ligand binding (MEPP). The theoretical foundation of MEPP is the conserved electrostatic potential difference (EPD) in cognate pairs of active site residues in proteins with the same functionality. Previously,

SUBMITTER: Chakraborty S 

PROVIDER: S-EPMC3597595 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature