Abstract
Replica exchange with solute tempering (REST) is a variant of the popular replica exchange (REX) method that is particularly suitable for enhanced sampling of protein conformational equilibria in explicit solvent. In REST, only the selected “solute” portion of the original Hamiltonian is scaled and subjected to effective tempering, requiring much fewer numbers of replicas for covering the same temperature range compared to the traditional REX. The efficiency of simulating protein folding ab initio even be further improved by REST2 where the energy gaps between low-to-high temperature replicas are narrowed to allow for more frequent reverse transitions as the solute-solvent interactions are weakened.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
