Asymmetric Behavior of Thymidylate Synthase Dimer Subunits in Denaturating Solvent Observed with Molecular Dynamics | Zendy

Filip Leonarski | Zendy; Monika Świniarska | Zendy; Andrzej Leś | Zendy

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Asymmetric Behavior of Thymidylate Synthase Dimer Subunits in Denaturating Solvent Observed with Molecular Dynamics

Author(s) -

Filip Leonarski,

Monika Świniarska,

Andrzej Leś

Publication year - 2015

Publication title -

computational biology journal

Language(s) - English

Resource type - Journals

eISSN - 2314-4173

pISSN - 2314-4165

DOI - 10.1155/2015/389018

Subject(s) - thymidylate synthase , guanidinium chloride , dimer , chemistry , molecular dynamics , urea , hydrochloride , guanidine , enzyme , denaturation (fissile materials) , crystallography , stereochemistry , solvent , biochemistry , computational chemistry , organic chemistry , biology , nuclear chemistry , fluorouracil , genetics , chemotherapy

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

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