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Article: Protein Dynamics Measurements by TROSY-Based NMR Experiments

TitleProtein Dynamics Measurements by TROSY-Based NMR Experiments
Authors
KeywordsNmr
Protein Dynamics
Relaxation
Trosy
Issue Date2000
PublisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/yjmre
Citation
Journal Of Magnetic Resonance, 2000, v. 143 n. 2, p. 423-426 How to Cite?
AbstractThe described TROSY-based experiments for investigating backbone dynamics of proteins make it possible to elucidate internal motions in large proteins via measurements of T 1, T 2, and NOE of backbone 15N nuclei. In our proposed sequences, the INEPT sequence is eliminated and the PEP sequence is replaced by the ST2-PT sequence from the HSQC-based experiments. This has the benefit of shortening the pulse sequences by 5.4 ms (=1/2J) and results in an increase in the intrinsic sensitivity of the proposed TROSY-based experiments. The TROSY-based experiments are on average of 13% more sensitive than the corresponding HSQC-based experiments on a uniformly 15N-labeled Xenopus laevis calcium-bound calmodulin sample on a 750-MHz spectrometer at 5°C. The amide proton linewidths of the TROSY-based experiments are 2-13 Hz narrower than those of the HSQC experiments. More sensitivity gain and higher resolution are expected if the protein sample is deuterated. © 2000 Academic Press.
Persistent Identifierhttp://hdl.handle.net/10722/157315
ISSN
2015 Impact Factor: 2.889
2015 SCImago Journal Rankings: 1.157
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorZhu, Gen_US
dc.contributor.authorXia, Yen_US
dc.contributor.authorNicholson, LKen_US
dc.contributor.authorSze, KHen_US
dc.date.accessioned2012-08-08T08:48:51Z-
dc.date.available2012-08-08T08:48:51Z-
dc.date.issued2000en_US
dc.identifier.citationJournal Of Magnetic Resonance, 2000, v. 143 n. 2, p. 423-426en_US
dc.identifier.issn1090-7807en_US
dc.identifier.urihttp://hdl.handle.net/10722/157315-
dc.description.abstractThe described TROSY-based experiments for investigating backbone dynamics of proteins make it possible to elucidate internal motions in large proteins via measurements of T 1, T 2, and NOE of backbone 15N nuclei. In our proposed sequences, the INEPT sequence is eliminated and the PEP sequence is replaced by the ST2-PT sequence from the HSQC-based experiments. This has the benefit of shortening the pulse sequences by 5.4 ms (=1/2J) and results in an increase in the intrinsic sensitivity of the proposed TROSY-based experiments. The TROSY-based experiments are on average of 13% more sensitive than the corresponding HSQC-based experiments on a uniformly 15N-labeled Xenopus laevis calcium-bound calmodulin sample on a 750-MHz spectrometer at 5°C. The amide proton linewidths of the TROSY-based experiments are 2-13 Hz narrower than those of the HSQC experiments. More sensitivity gain and higher resolution are expected if the protein sample is deuterated. © 2000 Academic Press.en_US
dc.languageengen_US
dc.publisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/yjmreen_US
dc.relation.ispartofJournal of Magnetic Resonanceen_US
dc.subjectNmren_US
dc.subjectProtein Dynamicsen_US
dc.subjectRelaxationen_US
dc.subjectTrosyen_US
dc.titleProtein Dynamics Measurements by TROSY-Based NMR Experimentsen_US
dc.typeArticleen_US
dc.identifier.emailSze, KH:khsze@hku.hken_US
dc.identifier.authoritySze, KH=rp00785en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1006/jmre.2000.2022en_US
dc.identifier.scopuseid_2-s2.0-0034170879en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0034170879&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume143en_US
dc.identifier.issue2en_US
dc.identifier.spage423en_US
dc.identifier.epage426en_US
dc.identifier.isiWOS:000086345400022-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridZhu, G=7402633110en_US
dc.identifier.scopusauthoridXia, Y=7403022398en_US
dc.identifier.scopusauthoridNicholson, LK=7102339460en_US
dc.identifier.scopusauthoridSze, KH=7006735061en_US
dc.identifier.citeulike3078674-

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