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

Figure 5

(a) Thymidylate synthase dimer 3D structure, colors represent 2D folds: red—-helix, yellow—-sheet, green—loops, blue molecule—ligands in the active site (not present in MD), and red beads—water. (b) TS structure with residues 88–118 (in both dimeric units) highlighted in black. (c) TS structure with residues 138–150 (in both dimeric units) highlighted in black. (d) TS structure with residues 180–200 (in both dimeric units) highlighted in black.

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