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Article: 2D and 3D TROSY-enhanced NOESY of 15N labeled proteins

Title2D and 3D TROSY-enhanced NOESY of 15N labeled proteins
Authors
Keywords15N Labeled Proteins
Noesy
Trosy
Issue Date1999
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, 1999, v. 14 n. 4, p. 377-381 How to Cite?
AbstractRecently, several TROSY-based experiments have been designed for backbone chemical shift assignment and measurement of the NOEs of 2H, 13C and 15N labeled proteins. Here, we present TROSY-enhanced NOESY experiments, namely the 2D S3E-NOESY-S3E, 3D TROSY-NOESY-S3E and S3E-NOESY-TROSY experiments. These experiments use the spin-state selective excitation method (S3E), and have the TROSY effect in all the indirectly and directly detected dimensions, and so provide optimal resolution for amide protons. The first two experiments provide an additional useful feature in that the diagonal peaks of the amide proton region are cancelled or greatly reduced, allowing clear identification of NOE cross peaks that are close to diagonal peaks.
Persistent Identifierhttp://hdl.handle.net/10722/157294
ISSN
2015 Impact Factor: 3.439
2015 SCImago Journal Rankings: 2.043
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorZhu, Gen_US
dc.contributor.authorXia, Yen_US
dc.contributor.authorSze, KHen_US
dc.contributor.authorYan, Xen_US
dc.date.accessioned2012-08-08T08:48:43Z-
dc.date.available2012-08-08T08:48:43Z-
dc.date.issued1999en_US
dc.identifier.citationJournal Of Biomolecular Nmr, 1999, v. 14 n. 4, p. 377-381en_US
dc.identifier.issn0925-2738en_US
dc.identifier.urihttp://hdl.handle.net/10722/157294-
dc.description.abstractRecently, several TROSY-based experiments have been designed for backbone chemical shift assignment and measurement of the NOEs of 2H, 13C and 15N labeled proteins. Here, we present TROSY-enhanced NOESY experiments, namely the 2D S3E-NOESY-S3E, 3D TROSY-NOESY-S3E and S3E-NOESY-TROSY experiments. These experiments use the spin-state selective excitation method (S3E), and have the TROSY effect in all the indirectly and directly detected dimensions, and so provide optimal resolution for amide protons. The first two experiments provide an additional useful feature in that the diagonal peaks of the amide proton region are cancelled or greatly reduced, allowing clear identification of NOE cross peaks that are close to diagonal peaks.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.subject15N Labeled Proteinsen_US
dc.subjectNoesyen_US
dc.subjectTrosyen_US
dc.title2D and 3D TROSY-enhanced NOESY of 15N labeled proteinsen_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.doi10.1023/A:1008386525465en_US
dc.identifier.scopuseid_2-s2.0-0032885432en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0032885432&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume14en_US
dc.identifier.issue4en_US
dc.identifier.spage377en_US
dc.identifier.epage381en_US
dc.identifier.isiWOS:000082504900009-
dc.publisher.placeNetherlandsen_US
dc.identifier.scopusauthoridZhu, G=7402633110en_US
dc.identifier.scopusauthoridXia, Y=7403022398en_US
dc.identifier.scopusauthoridSze, KH=7006735061en_US
dc.identifier.scopusauthoridYan, X=7403596605en_US
dc.identifier.citeulike3729185-

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