title: Opening the Arg-Glu salt bridge in myosin: computational study.
abstract: Opening the Arg-Glu salt bridge in myosin, which presumably succeeds the myosin-catalyzed hydrolysis of adenosine triphosphate, was modeled computationally on the basis of the structures corresponding to the enzyme-substrate and enzyme-product complexes found in the quantum mechanics-molecular mechanics simulations. According to the calculations of the potential of mean force, opening the bridge is considerably facilitated upon termination of the chemical reaction, but does not promote egress of inorganic phosphate by the back-door mechanism.
authors.affiliation: Department of Chemistry, M. V. Lomonosov Moscow State University, Moscow, 119992, Russian Federation.
authors.forename: Ilya
authors.initials: I
authors.lastname: Kaliman
authors.forename: Bella
authors.initials: B
authors.lastname: Grigorenko
authors.forename: Maria
authors.initials: M
authors.lastname: Shadrina
authors.forename: Alexander
authors.initials: A
authors.lastname: Nemukhin
mesh_terms: D001120:Arginine / Q000737:chemistry*; D003198:Computer Simulation; D018698:Glutamic Acid / Q000737:chemistry*; D008958:Models, Molecular; D009218:Myosins / Q000737:chemistry*; D011487:Protein Conformation; D011789:Quantum Theory; D013816:Thermodynamics
chemical_list: D018698:Glutamic Acid; D001120:Arginine; D009218:Myosins