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dc.contributor.authorYaşar, Fatih
dc.contributor.authorJiang ,Ping
dc.contributor.authorHansmann ,Ulrich H. E.
dc.date.accessioned2019-12-13T06:31:49Z
dc.date.available2019-12-13T06:31:49Z
dc.date.issued2014
dc.identifier.issn0295-5075
dc.identifier.urihttps://doi.org/10.1209/0295-5075/105/30008
dc.identifier.urihttp://hdl.handle.net/11655/18430
dc.description.abstractWe describe multicanonical molecular dynamic simulations of the N-terminal domain of the protein L9. Analyzing free energy landscapes and thermal ordering, we propose a possible folding mechanism for the protein. By comparing our results with that of molecular dynamics runs of the protein at constant temperature, we find that multicanonical molecular dynamics leads to orders of magnitude higher sampling of folding transitions. Copyright (c) EPLA, 2014
dc.language.isoen
dc.publisherIop Publishing Ltd
dc.relation.isversionof10.1209/0295-5075/105/30008
dc.rightsinfo:eu-repo/semantics/openAccess
dc.subjectPhysics
dc.titleMulticanonical Molecular Dynamics Simulations Of The N-Terminal Domain Of Protein L9
dc.typeinfo:eu-repo/semantics/article
dc.relation.journalEpl
dc.contributor.departmentFizik Mühendisliği
dc.identifier.volume105
dc.identifier.issue3
dc.description.indexWoS


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