Basin Hopping as a General and Versatile Optimization Framework for the Characterization of Biological Macromolecules
Figure 5
(a) The mean consecutive local minima distance is drawn against the lowest lRMSD obtained for each protein. (b and c) The lowest-lRMSD dimeric configuration (in opaque, with chains in different colors) is superimposed over the known native structure (in transparent) for the protein with native PDB ID 1c1y in (b) and 1g4y in (c). (d and e) The distribution of consecutive local minima distances in terms of lRMSD is shown in (d and e) for each of the proteins, respectively.
