Molecular mechanism of carbon nanotube to activate Subtilisin Carlsberg in polar and non-polar organic media.

ABSTRACT: In the work, we mainly used molecular dynamics (MD) simulation and protein structure network (PSN) to study subtilisin Carlsberg (SC) immobilized onto carbon nanotube (CNT) in water, acetonitrile and heptane solvents, in order to explore activation mechanism of enzymes in non-aqueous media. The result indicates that the affinity of SC with CNT follows the decreasing order of water > acetonitrile > heptane. The overall structure of SC and the catalytic triad display strong robustness to the change of environments, responsible for the activity retaining. However, the distances between two β-strands of substrate-binding pocket are significantly expanded by the immobilization in the increasing order of water < acetonitrile < heptane, contributing to the highest substrate-binding energy in hept

SUBMITTER: Zhang L 

PROVIDER: S-EPMC5118797 | biostudies-literature | 2016 Nov

REPOSITORIES: biostudies-literature