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- Publisher Website: 10.2174/092986611794653897
- Scopus: eid_2-s2.0-79951654698
- PMID: 21222637
- WOS: WOS:000289780100007
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Article: Probing protein dynamics by nuclear magnetic resonance
Title | Probing protein dynamics by nuclear magnetic resonance |
---|---|
Authors | |
Keywords | Nuclear magnetic resonance Paramagnetic relaxation enhancement Protein dynamics Relaxation dispersion Residual dipolar coupling |
Issue Date | 2011 |
Publisher | Bentham 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? |
Abstract | Proteins 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 Identifier | http://hdl.handle.net/10722/133608 |
ISSN | 2023 Impact Factor: 1.0 2023 SCImago Journal Rankings: 0.349 |
ISI Accession Number ID | |
References |
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Sze, KH | en_HK |
dc.contributor.author | Lai, PM | en_HK |
dc.date.accessioned | 2011-05-24T02:11:41Z | - |
dc.date.available | 2011-05-24T02:11:41Z | - |
dc.date.issued | 2011 | en_HK |
dc.identifier.citation | Protein And Peptide Letters, 2011, v. 18 n. 4, p. 373-379 | en_HK |
dc.identifier.issn | 0929-8665 | en_HK |
dc.identifier.uri | http://hdl.handle.net/10722/133608 | - |
dc.description.abstract | Proteins 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.language | eng | en_US |
dc.publisher | Bentham Science Publishers Ltd. The Journal's web site is located at http://www.bentham.org/ppl/index.htm | en_HK |
dc.relation.ispartof | Protein and Peptide Letters | en_HK |
dc.subject | Nuclear magnetic resonance | en_HK |
dc.subject | Paramagnetic relaxation enhancement | en_HK |
dc.subject | Protein dynamics | en_HK |
dc.subject | Relaxation dispersion | en_HK |
dc.subject | Residual dipolar coupling | en_HK |
dc.title | Probing protein dynamics by nuclear magnetic resonance | en_HK |
dc.type | Article | en_HK |
dc.identifier.openurl | http://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.email | Sze, KH:khsze@hku.hk | en_HK |
dc.identifier.authority | Sze, KH=rp00785 | en_HK |
dc.description.nature | link_to_subscribed_fulltext | - |
dc.identifier.doi | 10.2174/092986611794653897 | en_HK |
dc.identifier.pmid | 21222637 | - |
dc.identifier.scopus | eid_2-s2.0-79951654698 | en_HK |
dc.identifier.hkuros | 185372 | en_US |
dc.relation.references | http://www.scopus.com/mlt/select.url?eid=2-s2.0-79951654698&selection=ref&src=s&origin=recordpage | en_HK |
dc.identifier.volume | 18 | en_HK |
dc.identifier.issue | 4 | en_HK |
dc.identifier.spage | 373 | en_HK |
dc.identifier.epage | 379 | en_HK |
dc.identifier.isi | WOS:000289780100007 | - |
dc.publisher.place | Netherlands | en_HK |
dc.identifier.scopusauthorid | Sze, KH=7006735061 | en_HK |
dc.identifier.scopusauthorid | Lai, PM=37034286300 | en_HK |
dc.identifier.citeulike | 8844452 | - |
dc.identifier.issnl | 0929-8665 | - |