Skip to main content
U.S. Department of Energy
Office of Scientific and Technical Information

Force field parameters for S-nitrosocysteine and molecular dynamics simulations of S-nitrosated thioredoxin

Journal Article · · Biochemical and Biophysical Research Communications
 [1]
  1. Department of Biochemistry, Kangwon National University, Chunchon 200-701 (Korea, Republic of)

Estimation of structural perturbation induced by S-nitrosation is important to understand the mode of cellular signal transduction mediated by nitric oxide. Crystal structures of S-nitrosated proteins have been solved only for a few cases, however, so that molecular dynamics simulation may provide an alternative tool for probing structural perturbation. In this study AMBER-99 force field parameters for S-nitrosocysteine were developed and applied to molecular dynamics simulations of S-nitrosated thioredoxin. Geometry optimization at the level of HF/6-31G* was followed by a restrained electrostatic potential charge-fitting to obtain the atomic charges of S-nitrosocysteine. Force constants for bonds and angles were obtained from generalized AMBER force field. Torsional force constants for CC-SN and CS-NO were determined by fitting the torsional profiles obtained from geometry optimization with those from molecular mechanical energy minimization. Finally molecular dynamics simulations were performed with theses parameters on oxidized and reduced thioredoxin with and without S-nitrosocysteine. In all cases the root-mean-square deviations of {alpha}-carbons yielded well-behaved trajectories. The CC-SH dihedral angle which fluctuated severely during the simulation became quiet upon S-nitrosation. In conclusion the force field parameters developed in this study for S-nitrosocysteine appear to be suitable for molecular dynamics simulations of S-nitrosated proteins.

OSTI ID:
21255786
Journal Information:
Biochemical and Biophysical Research Communications, Journal Name: Biochemical and Biophysical Research Communications Journal Issue: 2 Vol. 377; ISSN 0006-291X; ISSN BBRCA9
Country of Publication:
United States
Language:
English

Similar Records

Force field dependence of NMR-based restrained molecular dynamics DNA structure calculations including an analysis of the influence of residual dipolar coupling restraints
Journal Article · Thu Jun 16 00:00:00 EDT 2005 · Journal of Biomolecular Structure and Dynamics · OSTI ID:840902

Force field parameter estimation of functional perfluoropolyether lubricants
Journal Article · Fri Dec 31 23:00:00 EST 2010 · Journal of Applied Physics · OSTI ID:1015225

Force Field Parameter Estimation of Functional Perfluoropolyether Lubricants
Journal Article · Fri Dec 31 23:00:00 EST 2010 · Journal of Applied Physics · OSTI ID:1010918