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Article: Probing protein dynamics by nuclear magnetic resonance

TitleProbing protein dynamics by nuclear magnetic resonance
Authors
KeywordsNuclear magnetic resonance
Paramagnetic relaxation enhancement
Protein dynamics
Relaxation dispersion
Residual dipolar coupling
Issue Date2011
PublisherBentham Science Publishers Ltd. The Journal's web site is located at http://www.bentham.org/ppl/index.htm
Citation
Protein And Peptide Letters, 2011, v. 18 n. 4, p. 373-379 How to Cite?
AbstractProteins are dynamic molecules that often undergo conformational changes while performing their specific functions, such as target recognition, ligand binding and catalysis. NMR spectroscopy is uniquely suited to study protein dynamics, because site-specific information can be obtained for motions that span a broad range of time scales. The information obtained from NMR dynamics experiments has provided insights into specific structural changes or conformational energetics associated with molecular function. In the last decade, a number of new advancements in NMR methodologies have further extended our ability to characterize protein dynamics. Here, we present an overview of current NMR technology that is used to monitor the dynamic properties of proteins. © 2011 Bentham Science Publishers Ltd.
Persistent Identifierhttp://hdl.handle.net/10722/133608
ISSN
2015 Impact Factor: 1.069
2015 SCImago Journal Rankings: 0.472
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorSze, KHen_HK
dc.contributor.authorLai, PMen_HK
dc.date.accessioned2011-05-24T02:11:41Z-
dc.date.available2011-05-24T02:11:41Z-
dc.date.issued2011en_HK
dc.identifier.citationProtein And Peptide Letters, 2011, v. 18 n. 4, p. 373-379en_HK
dc.identifier.issn0929-8665en_HK
dc.identifier.urihttp://hdl.handle.net/10722/133608-
dc.description.abstractProteins are dynamic molecules that often undergo conformational changes while performing their specific functions, such as target recognition, ligand binding and catalysis. NMR spectroscopy is uniquely suited to study protein dynamics, because site-specific information can be obtained for motions that span a broad range of time scales. The information obtained from NMR dynamics experiments has provided insights into specific structural changes or conformational energetics associated with molecular function. In the last decade, a number of new advancements in NMR methodologies have further extended our ability to characterize protein dynamics. Here, we present an overview of current NMR technology that is used to monitor the dynamic properties of proteins. © 2011 Bentham Science Publishers Ltd.en_HK
dc.languageengen_US
dc.publisherBentham Science Publishers Ltd. The Journal's web site is located at http://www.bentham.org/ppl/index.htmen_HK
dc.relation.ispartofProtein and Peptide Lettersen_HK
dc.subjectNuclear magnetic resonanceen_HK
dc.subjectParamagnetic relaxation enhancementen_HK
dc.subjectProtein dynamicsen_HK
dc.subjectRelaxation dispersionen_HK
dc.subjectResidual dipolar couplingen_HK
dc.titleProbing protein dynamics by nuclear magnetic resonanceen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0929-8665&volume=18&issue=4&spage=373&epage=379&date=2011&atitle=Probing+protein+dynamics+by+nuclear+magnetic+resonance-
dc.identifier.emailSze, KH:khsze@hku.hken_HK
dc.identifier.authoritySze, KH=rp00785en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.2174/092986611794653897en_HK
dc.identifier.pmid21222637-
dc.identifier.scopuseid_2-s2.0-79951654698en_HK
dc.identifier.hkuros185372en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-79951654698&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume18en_HK
dc.identifier.issue4en_HK
dc.identifier.spage373en_HK
dc.identifier.epage379en_HK
dc.identifier.isiWOS:000289780100007-
dc.publisher.placeNetherlandsen_HK
dc.identifier.scopusauthoridSze, KH=7006735061en_HK
dc.identifier.scopusauthoridLai, PM=37034286300en_HK
dc.identifier.citeulike8844452-

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