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dc.contributor.authorJiang, Zhongling
dc.contributor.authorZhang, Bin
dc.date.accessioned2020-11-16T22:38:48Z
dc.date.available2020-11-16T22:38:48Z
dc.date.issued2019-11
dc.date.submitted2019-04
dc.identifier.issn0031-9007
dc.identifier.issn1079-7114
dc.identifier.urihttps://hdl.handle.net/1721.1/128497
dc.description.abstractNucleosome positioning controls the accessible regions of chromatin and plays essential roles in DNA-Templated processes. ATP driven remodeling enzymes are known to be crucial for its establishment in vivo, but their nonequilibrium nature has hindered the development of a unified theoretical framework for nucleosome positioning. Using a perturbation theory, we show that the effect of these enzymes can be well approximated by effective equilibrium models with rescaled temperatures and interactions. Numerical simulations support the accuracy of the theory in predicting both kinetic and steady-state quantities, including the effective temperature and the radial distribution function, in biologically relevant regimes. The energy landscape view emerging from our study provides an intuitive understanding for the impact of remodeling enzymes in either reinforcing or overwriting intrinsic signals for nucleosome positioning, and may help improve the accuracy of computational models for its prediction in silico.en_US
dc.description.sponsorshipNational Institutes of Health (Grant 1R35GM133580-01)en_US
dc.language.isoen
dc.publisherAmerican Physical Society (APS)en_US
dc.relation.isversionofhttp://dx.doi.org/10.1103/physrevlett.123.208102en_US
dc.rightsArticle is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use.en_US
dc.sourceAPSen_US
dc.titleTheory of Active Chromatin Remodelingen_US
dc.typeArticleen_US
dc.identifier.citationJiang, Zhongling and Bin Zhang. "Theory of Active Chromatin Remodeling." Physical Review Letters 123, 20 (November 2019): 208102 © 2019 American Physical Societyen_US
dc.contributor.departmentMassachusetts Institute of Technology. Department of Chemistryen_US
dc.relation.journalPhysical Review Lettersen_US
dc.eprint.versionFinal published versionen_US
dc.type.urihttp://purl.org/eprint/type/JournalArticleen_US
eprint.statushttp://purl.org/eprint/status/PeerRevieweden_US
dc.date.updated2020-09-22T16:16:47Z
dspace.date.submission2020-09-22T16:16:49Z
mit.journal.volume123en_US
mit.journal.issue20en_US
mit.licensePUBLISHER_POLICY
mit.metadata.statusComplete


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