Role of Resultant Dipole Moment in Mechanical Dissociation of Biological Complexes.

ABSTRACT: Protein-peptide interactions play essential roles in many cellular processes and their structural characterization is the major focus of current experimental and theoretical research. Two decades ago, it was proposed to employ the steered molecular dynamics (SMD) to assess the strength of protein-peptide interactions. The idea behind using SMD simulations is that the mechanical stability can be used as a promising and an efficient alternative to computationally highly demanding estimation of binding affinity. However, mechanical stability defined as a peak in force-extension profile depends on the choice of the pulling direction. Here we propose an uncommon choice of the pulling direction along resultant dipole moment (RDM) vector, which has not been explored in SMD simulations so far. Usi

SUBMITTER: Kouza M 

PROVIDER: S-EPMC6222447 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature