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- Publisher Website: 10.1023/A:1026590201757
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- PMID: 11142516
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Article: Transverse relaxation optimized 3D and 4D 15N/ 15N separated NOESY experiments of 15N labeled proteins
Title | Transverse relaxation optimized 3D and 4D 15N/ 15N separated NOESY experiments of 15N labeled proteins |
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Authors | |
Keywords | 15N labeled protein HSQC NOESY TROSY |
Issue Date | 2000 |
Publisher | Springer 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? |
Abstract | NMR 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 Identifier | http://hdl.handle.net/10722/157307 |
ISSN | 2023 Impact Factor: 2.4 2023 SCImago Journal Rankings: 0.817 |
ISI Accession Number ID | |
References |
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Xia, Y | en_US |
dc.contributor.author | Sze, K | en_US |
dc.contributor.author | Zhu, G | en_US |
dc.date.accessioned | 2012-08-08T08:48:48Z | - |
dc.date.available | 2012-08-08T08:48:48Z | - |
dc.date.issued | 2000 | en_US |
dc.identifier.citation | Journal Of Biomolecular Nmr, 2000, v. 18 n. 3, p. 261-268 | en_US |
dc.identifier.issn | 0925-2738 | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/157307 | - |
dc.description.abstract | NMR 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.language | eng | en_US |
dc.publisher | Springer Verlag Dordrecht. The Journal's web site is located at http://springerlink.metapress.com/openurl.asp?genre=journal&issn=0925-2738 | en_US |
dc.relation.ispartof | Journal of Biomolecular NMR | en_US |
dc.subject | 15N labeled protein | - |
dc.subject | HSQC | - |
dc.subject | NOESY | - |
dc.subject | TROSY | - |
dc.subject.mesh | Deuterium | en_US |
dc.subject.mesh | Magnetics - Diagnostic Use | en_US |
dc.subject.mesh | Nitrogen Isotopes - Diagnostic Use | en_US |
dc.subject.mesh | Nuclear Magnetic Resonance, Biomolecular - Methods | en_US |
dc.subject.mesh | Plant Proteins - Chemistry | en_US |
dc.subject.mesh | Protein Structure, Tertiary | en_US |
dc.subject.mesh | Proteins - Chemistry | en_US |
dc.subject.mesh | Sensitivity And Specificity | en_US |
dc.subject.mesh | Time Factors | en_US |
dc.subject.mesh | Trichosanthin - Chemistry | en_US |
dc.title | Transverse relaxation optimized 3D and 4D 15N/ 15N separated NOESY experiments of 15N labeled proteins | en_US |
dc.type | Article | en_US |
dc.identifier.email | Sze, K:khsze@hku.hk | en_US |
dc.identifier.authority | Sze, K=rp00785 | en_US |
dc.description.nature | link_to_subscribed_fulltext | en_US |
dc.identifier.doi | 10.1023/A:1026590201757 | - |
dc.identifier.pmid | 11142516 | - |
dc.identifier.scopus | eid_2-s2.0-0033636799 | en_US |
dc.relation.references | http://www.scopus.com/mlt/select.url?eid=2-s2.0-0033636799&selection=ref&src=s&origin=recordpage | en_US |
dc.identifier.volume | 18 | en_US |
dc.identifier.issue | 3 | en_US |
dc.identifier.spage | 261 | en_US |
dc.identifier.epage | 268 | en_US |
dc.identifier.isi | WOS:000165485200009 | - |
dc.publisher.place | Netherlands | en_US |
dc.identifier.scopusauthorid | Xia, Y=7403022398 | en_US |
dc.identifier.scopusauthorid | Sze, K=7006735061 | en_US |
dc.identifier.scopusauthorid | Zhu, G=7402633110 | en_US |
dc.identifier.issnl | 0925-2738 | - |