TY - JOUR A2 - Mezei, Mihaly AU - Leonarski, Filip AU - Świniarska, Monika AU - Leś, Andrzej PY - 2015 DA - 2015/03/11 TI - Asymmetric Behavior of Thymidylate Synthase Dimer Subunits in Denaturating Solvent Observed with Molecular Dynamics SP - 389018 VL - 2015 AB - 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 dimericenzyme undergoes partial unfolding asymmetrically. It was shown also that urea is a better denaturant inthe 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 inthe literature activity of thymidylate synthase through a half-the-site mechanism. SN - 2314-4165 UR - https://doi.org/10.1155/2015/389018 DO - 10.1155/2015/389018 JF - Computational Biology Journal PB - Hindawi Publishing Corporation KW - ER -