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dc.contributorVirginia Techen
dc.contributor.authorWu, Z. H.en
dc.contributor.authorXing, Jianhuaen
dc.date.accessioned2014-02-26T19:10:03Zen
dc.date.available2014-02-26T19:10:03Zen
dc.date.issued2012-11en
dc.identifier.citationWu, Zhanghan; Xing, Jianhua, "Functional Roles of Slow Enzyme Conformational Changes in Network Dynamics," Biophysical Journal 103(5), 1052-1059 (2012); doi: 10.1016/j.bpj.2012.08.008en
dc.identifier.issn0006-3495en
dc.identifier.urihttp://hdl.handle.net/10919/25759en
dc.description.abstractExtensive studies from different fields reveal that many macromolecules, especially enzymes, show slow transitions among different conformations. This phenomenon is named such things as dynamic disorder, heterogeneity, hysteretic or mnemonic enzymes across these different fields, and has been directly demonstrated by single molecule enzymology and NMR studies recently. We analyzed enzyme slow conformational changes in the context of regulatory networks. A single enzymatic reaction with slow conformational changes can filter upstream network noises, and can either resonantly respond to the system stimulus at certain frequencies or respond adaptively for sustained input signals of the network fluctuations. It thus can serve as a basic functional motif with properties that are normally for larger intermolecular networks in the field of systems biology. We further analyzed examples including enzymes functioning against pH fluctuations, metabolic state change of Artemia embryos, and kinetic insulation of fluctuations in metabolic networks. The study also suggests that hysteretic enzymes may be building blocks of synthetic networks with various properties such as narrow-banded filtering. The work fills the missing gap between studies on enzyme biophysics and network level dynamics, and reveals that the coupling between the two is functionally important; it also suggests that the conformational dynamics of some enzymes may be evolutionally selected.en
dc.description.sponsorshipNational Science Foundation grant EF-1038636en
dc.language.isoen_USen
dc.publisherCELL PRESSen
dc.rightsIn Copyrighten
dc.rights.urihttp://rightsstatements.org/vocab/InC/1.0/en
dc.subjectleaf nitrate reductaseen
dc.subjectsingle-moleculeen
dc.subjectpositive feedbacken
dc.subjectescherichia-colien
dc.subjectprotein dynamicsen
dc.subjectintracellular phen
dc.subjectnoiseen
dc.subjectcatalysisen
dc.subjectbehavioren
dc.subjectbindingen
dc.titleFunctional Roles of Slow Enzyme Conformational Changes in Network Dynamicsen
dc.typeArticle - Refereeden
dc.contributor.departmentBiological Sciencesen
dc.identifier.urlhttp://www.sciencedirect.com/science/article/pii/S0006349512008685en
dc.date.accessed2014-02-05en
dc.title.serialBiophysical Journalen
dc.identifier.doihttps://doi.org/10.1016/j.bpj.2012.08.008en


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