Figure 8.

Simple structure-based expectations of quartet peak positions for a symmetric dimer such as thymidylate synthase. Ligand is shown as a filled black circle for each lig₁ state shown. The residue amide giving rise to the 2D peaks are shown as red and green squares, corresponding to the bound and empty subunits, respectively. Conformational change in a protomer is indicated by jagged lines at the interface. Panels indicate conformational change in the binding protomer only (A), both protomers (B), and in neither (C).