Molecular Dynamics Simulations and NMR Experimental Study of Oxidized Glutathione in Aqueous Solution

Abstract

All-atom molecular simulations and NMR experiments have been used to study the conformations and interactions of oxidized glutathione (GSSG) in aqueous solution. The simulations are characterized by the radius of gyration, intramolecular distance, root-meansquare deviation and solvent-accessible surface area. The variations in these properties show time dependences. Interestingly, the two chains connected by the disulfide linkage in GSSG show different flexibilities in aqueous solution. The conformations of GSSG can convert from "extended" to "folded" states. Also, the two different kinds of amide hydrogen atoms in cysteine (Cys) and glycin (Gly) show different capabilities in forming N-H· · ·O hydrogen bonds with water molecules. Temperature-dependent NMR results show agreements with the MD simulations.

Studies on the Conformations and Hydrogen-Bonding Interactions of RGD Tri-peptide in Aqueous Solutions by Molecular Dynamics Simulations and 2D-NOESY Spectroscopy

“…In previous papers, we have studied the conformations and interactions in the special associate system such as amide-water and small peptide mixtures. Some interesting phenomena were observed in the mixture, such as weak C-HÁÁÁO contacts and changes of the conformations [21][22][23].…”