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Article: Transverse relaxation optimized 3D and 4D 15N/ 15N separated NOESY experiments of 15N labeled proteins

TitleTransverse relaxation optimized 3D and 4D 15N/ 15N separated NOESY experiments of 15N labeled proteins
Authors
Issue Date2000
PublisherSpringer Verlag Dordrecht. The Journal's web site is located at http://springerlink.metapress.com/openurl.asp?genre=journal&issn=0925-2738
Citation
Journal Of Biomolecular Nmr, 2000, v. 18 n. 3, p. 261-268 How to Cite?
AbstractNMR studies of protein structures require knowledge of spectral assignments through correlation spectroscopy and the measurement of dipolar interactions by NOESY-type experiments. In order to obtain NOEs for protons with degenerate chemical shifts, which is particularly common for large proteins with significant helical content, 3D and 4D 15N/ 15N separated NOESY experiments (HSQC-NOESY-HSQC) are essential for NMR studies of these proteins. TROSY sections could replace the latter or both HSQC parts of the 3D and 4D 15N/ 15N separated HSQC-NOESY-HSQC pulse sequences tO enhance signal sensitivity and improve resolution. For a 1.0 mM, 100% 15N and 70% 2H-labeled Trichosanthin sample (~27 kDa) at 5 °C it is found that sensitivity enhancements could only be obtained when TROSY sections replace the latter HSQC parts of 3D and 4D 15N/ 15N separated HSQC-NOESY-HSQC pulse sequences. The sensitivities of 3D and 4D HSQC-NOESY-TROSY experiments are enhanced by 62% and 8% at 5 °C, respectively, compared to their corresponding: 3D and 4D HSQC-NOESY-HSQC experiments. Furthermore, the corresponding linewidths are, on average, decreased by 20% and 18% Hz in the H(N) and N2 dimensions, respectively. This enhancement of sensitivity depends on the molecular mass of the sample used and the lengths of the evolution times in the indirectly and directly detected dimensions.
Persistent Identifierhttp://hdl.handle.net/10722/157307
ISSN
2015 Impact Factor: 3.439
2015 SCImago Journal Rankings: 2.043
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorXia, Yen_US
dc.contributor.authorSze, Ken_US
dc.contributor.authorZhu, Gen_US
dc.date.accessioned2012-08-08T08:48:48Z-
dc.date.available2012-08-08T08:48:48Z-
dc.date.issued2000en_US
dc.identifier.citationJournal Of Biomolecular Nmr, 2000, v. 18 n. 3, p. 261-268en_US
dc.identifier.issn0925-2738en_US
dc.identifier.urihttp://hdl.handle.net/10722/157307-
dc.description.abstractNMR studies of protein structures require knowledge of spectral assignments through correlation spectroscopy and the measurement of dipolar interactions by NOESY-type experiments. In order to obtain NOEs for protons with degenerate chemical shifts, which is particularly common for large proteins with significant helical content, 3D and 4D 15N/ 15N separated NOESY experiments (HSQC-NOESY-HSQC) are essential for NMR studies of these proteins. TROSY sections could replace the latter or both HSQC parts of the 3D and 4D 15N/ 15N separated HSQC-NOESY-HSQC pulse sequences tO enhance signal sensitivity and improve resolution. For a 1.0 mM, 100% 15N and 70% 2H-labeled Trichosanthin sample (~27 kDa) at 5 °C it is found that sensitivity enhancements could only be obtained when TROSY sections replace the latter HSQC parts of 3D and 4D 15N/ 15N separated HSQC-NOESY-HSQC pulse sequences. The sensitivities of 3D and 4D HSQC-NOESY-TROSY experiments are enhanced by 62% and 8% at 5 °C, respectively, compared to their corresponding: 3D and 4D HSQC-NOESY-HSQC experiments. Furthermore, the corresponding linewidths are, on average, decreased by 20% and 18% Hz in the H(N) and N2 dimensions, respectively. This enhancement of sensitivity depends on the molecular mass of the sample used and the lengths of the evolution times in the indirectly and directly detected dimensions.en_US
dc.languageengen_US
dc.publisherSpringer Verlag Dordrecht. The Journal's web site is located at http://springerlink.metapress.com/openurl.asp?genre=journal&issn=0925-2738en_US
dc.relation.ispartofJournal of Biomolecular NMRen_US
dc.subject.meshDeuteriumen_US
dc.subject.meshMagnetics - Diagnostic Useen_US
dc.subject.meshNitrogen Isotopes - Diagnostic Useen_US
dc.subject.meshNuclear Magnetic Resonance, Biomolecular - Methodsen_US
dc.subject.meshPlant Proteins - Chemistryen_US
dc.subject.meshProtein Structure, Tertiaryen_US
dc.subject.meshProteins - Chemistryen_US
dc.subject.meshSensitivity And Specificityen_US
dc.subject.meshTime Factorsen_US
dc.subject.meshTrichosanthin - Chemistryen_US
dc.titleTransverse relaxation optimized 3D and 4D 15N/ 15N separated NOESY experiments of 15N labeled proteinsen_US
dc.typeArticleen_US
dc.identifier.emailSze, K:khsze@hku.hken_US
dc.identifier.authoritySze, K=rp00785en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.pmid11142516-
dc.identifier.scopuseid_2-s2.0-0033636799en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0033636799&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume18en_US
dc.identifier.issue3en_US
dc.identifier.spage261en_US
dc.identifier.epage268en_US
dc.identifier.isiWOS:000165485200009-
dc.publisher.placeNetherlandsen_US
dc.identifier.scopusauthoridXia, Y=7403022398en_US
dc.identifier.scopusauthoridSze, K=7006735061en_US
dc.identifier.scopusauthoridZhu, G=7402633110en_US

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