Asymmetric Behavior of Thymidylate Synthase Dimer Subunits in Denaturating Solvent Observed with Molecular Dynamics. (11th March 2015)

• Record Type: Journal Article
• Authors: Leonarski, Filip; Świniarska, Monika; Leś, Andrzej
• Other Names: Mezei Mihaly Academic Editor.
• Is Part Of: Computational biology journal. Volume 2015(2015)
• Publication Date: 2015-03-11
• Subjects: Computational biology -- Periodicals; Computational biology; Biología -- Publicaciones periódicas; Ciencias -- Publicaciones periódicas; Periodicals; Electronic journals; 570.285
• DOI: 10.1155/2015/389018
• Languages: English
• ISSNs: 2314-4165

Abstract

Abstract : A molecular dynamics simulations of the thymidylate synthase denaturation in chaotrope solvents (urea, guanidinium hydrochloride) were performed on 600 ns timescale. It appeared that this dimeric enzyme undergoes partial unfolding asymmetrically. It was shown also that urea is a better denaturant in the MD condition, as compared to guanidinium chloride. The unfolding occurs first at the external helices (AA 88-118) and follows by the AA 188-200 region. The present results correspond to the suggested in the literature activity of thymidylate synthase through a half-the-site mechanism.