dc.contributor.author | Jiang, Ping | |
dc.contributor.author | Yaşar, Fatih | |
dc.contributor.author | Hansmann, Ulrich H. E. | |
dc.date.accessioned | 2019-12-13T06:34:33Z | |
dc.date.available | 2019-12-13T06:34:33Z | |
dc.date.issued | 2013 | |
dc.identifier.issn | 1549-9618 | |
dc.identifier.uri | https://doi.org/10.1021/ct400312d | |
dc.identifier.uri | http://hdl.handle.net/11655/18454 | |
dc.description.abstract | We compare the efficiency of multicanonical and replica exchange molecular dynamics for the sampling of folding/unfolding events in simulations of proteins with end-to-end beta-sheet. In Go-model simulations of the 75-residue MNK6, we observe improvement factors of 30 in the number of folding/unfolding events of multicanonical molecular dynamics over replica exchange molecular dynamics. As an application, we use this enhanced sampling to study the folding landscape of the 36-residue DS119 with an all-atom physical force field and implicit solvent. Here, we find that the rate-limiting step is the formation of the central helix that then provides a scaffold for the parallel beta-sheet formed by the two chain ends. | |
dc.language.iso | en | |
dc.publisher | Amer Chemical Soc | |
dc.relation.isversionof | 10.1021/ct400312d | |
dc.rights | info:eu-repo/semantics/openAccess | |
dc.subject | Chemistry | |
dc.subject | Physics | |
dc.title | Sampling of Protein Folding Transitions: Multicanonical Versus Replica Exchange Molecular Dynamics | |
dc.type | info:eu-repo/semantics/article | |
dc.type | info:eu-repo/semantics/publishedVersion | |
dc.relation.journal | Journal Of Chemical Theory And Computation | |
dc.contributor.department | Fizik Mühendisliği | |
dc.identifier.volume | 9 | |
dc.identifier.issue | 8 | |
dc.identifier.startpage | 3816 | |
dc.identifier.endpage | 3825 | |
dc.description.index | WoS | |