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Article: Water permeation dynamics of AqpZ: A tale of two states

TitleWater permeation dynamics of AqpZ: A tale of two states
Authors
Issue Date2011
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/bbamem
Citation
Biochimica Et Biophysica Acta - Biomembranes, 2011, v. 1808 n. 6, p. 1581-1586 How to Cite?
AbstractMolecular dynamics simulations of aquaporin Z homotetramer which is a membrane protein facilitating rapid water movement through the plasma membrane of Escherichia coli were performed. Initial configurations were taken from the open and closed states of crystal structures separately. The resulting water osmotic permeability (p f) and diffusive permeability (p d) displayed distinct features. Consistent with previous studies, the side chain conformation of arginine189 was found to mediate the water permeability. A potential of mean force (PMF) as a function of the distance between NH1 of R189 and carbonyl oxygen of A117 was constructed based on the umbrella sampling technique. There are multiple local minima and transition states on the PMF. The assignment of the open or closed state was supported by the permeability p f, calculated within trajectories in umbrella sampling simulations. Our study disclosed a detailed mechanism of the gated water transport. © 2011 Elsevier B.V. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/185399
ISSN
2015 Impact Factor: 3.687
2015 SCImago Journal Rankings: 1.769
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorXin, Len_US
dc.contributor.authorSu, Hen_US
dc.contributor.authorNielsen, CHen_US
dc.contributor.authorTang, Cen_US
dc.contributor.authorTorres, Jen_US
dc.contributor.authorMu, Yen_US
dc.date.accessioned2013-07-30T07:32:15Z-
dc.date.available2013-07-30T07:32:15Z-
dc.date.issued2011en_US
dc.identifier.citationBiochimica Et Biophysica Acta - Biomembranes, 2011, v. 1808 n. 6, p. 1581-1586en_US
dc.identifier.issn0005-2736en_US
dc.identifier.urihttp://hdl.handle.net/10722/185399-
dc.description.abstractMolecular dynamics simulations of aquaporin Z homotetramer which is a membrane protein facilitating rapid water movement through the plasma membrane of Escherichia coli were performed. Initial configurations were taken from the open and closed states of crystal structures separately. The resulting water osmotic permeability (p f) and diffusive permeability (p d) displayed distinct features. Consistent with previous studies, the side chain conformation of arginine189 was found to mediate the water permeability. A potential of mean force (PMF) as a function of the distance between NH1 of R189 and carbonyl oxygen of A117 was constructed based on the umbrella sampling technique. There are multiple local minima and transition states on the PMF. The assignment of the open or closed state was supported by the permeability p f, calculated within trajectories in umbrella sampling simulations. Our study disclosed a detailed mechanism of the gated water transport. © 2011 Elsevier B.V. All rights reserved.en_US
dc.languageengen_US
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/bbamemen_US
dc.relation.ispartofBiochimica et Biophysica Acta - Biomembranesen_US
dc.subject.meshAlanine - Chemistry - Genetics - Metabolismen_US
dc.subject.meshAmino Acid Substitutionen_US
dc.subject.meshAquaporins - Chemistry - Genetics - Metabolismen_US
dc.subject.meshArginine - Chemistry - Genetics - Metabolismen_US
dc.subject.meshBiological Transporten_US
dc.subject.meshCell Membrane - Metabolismen_US
dc.subject.meshCell Membrane Permeabilityen_US
dc.subject.meshEscherichia Coli - Metabolismen_US
dc.subject.meshEscherichia Coli Proteins - Chemistry - Genetics - Metabolismen_US
dc.subject.meshModels, Molecularen_US
dc.subject.meshMolecular Dynamics Simulationen_US
dc.subject.meshMutationen_US
dc.subject.meshOsmosisen_US
dc.subject.meshOsmotic Pressureen_US
dc.subject.meshProtein Conformationen_US
dc.subject.meshSerine - Chemistry - Genetics - Metabolismen_US
dc.subject.meshWater - Chemistry - Metabolismen_US
dc.titleWater permeation dynamics of AqpZ: A tale of two statesen_US
dc.typeArticleen_US
dc.identifier.emailTang, C: tangc@hku.hken_US
dc.identifier.authorityTang, C=rp01765en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/j.bbamem.2011.02.001en_US
dc.identifier.pmid21315687en_US
dc.identifier.scopuseid_2-s2.0-79954774036en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-79954774036&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume1808en_US
dc.identifier.issue6en_US
dc.identifier.spage1581en_US
dc.identifier.epage1586en_US
dc.identifier.isiWOS:000290705700019-
dc.publisher.placeNetherlandsen_US
dc.identifier.scopusauthoridXin, L=35075384700en_US
dc.identifier.scopusauthoridSu, H=55224470200en_US
dc.identifier.scopusauthoridNielsen, CH=9738511400en_US
dc.identifier.scopusauthoridTang, C=35489259800en_US
dc.identifier.scopusauthoridTorres, J=7402798449en_US
dc.identifier.scopusauthoridMu, Y=7103374032en_US

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