Motor-like Properties of Nonmotor Enzymes.

ABSTRACT: Molecular motors are thought to generate force and directional motion via nonequilibrium switching between energy surfaces. Because all enzymes can undergo such switching, we hypothesized that the ability to generate rotary motion and torque is not unique to highly adapted biological motor proteins but is instead a common feature of enzymes. We used molecular dynamics simulations to compute energy surfaces for hundreds of torsions in three enzymes-adenosine kinase, protein kinase A, and HIV-1 protease-and used these energy surfaces within a kinetic model that accounts for intersurface switching and intrasurface probability flows. When substrate is out of equilibrium with product, we find computed torsion rotation rates up ∼140 cycles s^-1, with stall torques up to ∼2 kcal mol

SUBMITTER: Slochower DR 

PROVIDER: S-EPMC5961456 | biostudies-literature | 2018 May

REPOSITORIES: biostudies-literature