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

Figure 1

Root mean square deviation in reference to starting structure (black) calculated between carbon coordinates of the first dimeric subunit versus the second subunit (intermonomer RMSD red) of the thymidylate synthase in function of time for 300 ns molecular dynamics simulation. Raise of the intermonomer RMSD value shows asymmetric unfolding of the subunits, especially in case of urea.