FIGURE 1.

DXMS reveals regions of disorder in MutS. A, percentage deuterium incorporation for individual peptides of MutS after 30 (black) or 300 s (green) are shown as bars spanning over the indicated sequence on the x axis. Regions containing peptides that fully exchange rapidly or do not exchange at all are boxed. B, kinetics of deuteron incorporation for a representative peptide from each region boxed in A. C, regions containing extremely rapidly (red) or slowly (blue) exchanging peptides mapped onto the six domains of the MutS monomer are distinguished by color on a ribbon diagram constructed from the x-ray structures of residues 1–800 (Protein Data Bank code 1e3m (5)) and 820–853 (Protein Data Bank code 2ok2 (32)) with a linker of arbitrary conformation. D, regions from above are mapped onto a MutS dimer (right), and regions 8–10 are mapped onto a ribbon diagram of the ATPase domain (left).