Conformational diversity induces nanosecond-timescale chemical disorder in the HIV-1 protease reaction pathway.

ABSTRACT: The role of conformational diversity in enzyme catalysis has been a matter of analysis in recent studies. Pre-organization of the active site has been pointed out as the major source for enzymes' catalytic power. Following this line of thought, it is becoming clear that specific, instantaneous, non-rare enzyme conformations that make the active site perfectly pre-organized for the reaction lead to the lowest activation barriers that mostly contribute to the macroscopically observed reaction rate. The present work is focused on exploring the relationship between structure and catalysis in HIV-1 protease (PR) with an adiabatic mapping method, starting from different initial structures, collected from a classical MD simulation. The first, rate-limiting step of the HIV-1 PR catalytic mechanism

SUBMITTER: Calixto AR 

PROVIDER: S-EPMC6677113 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature