title: Replica exchange with solute tempering: efficiency in large scale systems.
abstract: We apply the recently developed replica exchange with solute tempering (REST) to three large solvated peptide systems: an alpha-helix, a beta-hairpin, and a TrpCage, with these peptides defined as the "central group". We find that our original implementation of REST is not always more efficient than the replica exchange method (REM). Specifically, we find that exchanges between folded (F) and unfolded (U) conformations with vastly different structural energies are greatly reduced by the nonappearance of the water self-interaction energy in the replica exchange acceptance probabilities. REST, however, is expected to remain useful for a large class of systems for which the energy gap between the two states is not large, such as weakly bound protein-ligand complexes. Alternatively, a shell of water molecules can be incorporated into the central group, as discussed in the original paper.
authors: Department of Chemistry, Columbia University, New York, New York 10027, USA.
authors: Xuhui
authors: X
authors: Huang
authors: Morten
authors: M
authors: Hagen
authors: Byungchan
authors: B
authors: Kim
authors: Richard A
authors: RA
authors: Friesner
authors: Ruhong
authors: R
authors: Zhou
authors: B J
authors: BJ
authors: Berne
mesh_terms: D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D017510:Protein Folding; D016628:Replica Techniques / Q000379:methods*; D014867:Water / Q000737:chemistry
chemical_list: D010455:Peptides; D014867:Water