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Article: Clean SEA-HSQC: A method to map solvent exposed amides in large non-deuterated proteins with gradient-enhanced HSQC

TitleClean SEA-HSQC: A method to map solvent exposed amides in large non-deuterated proteins with gradient-enhanced HSQC
Authors
KeywordsAmide Hydrogen Exchange
Clean-Pm
Hsqc
Proteins
Resonance Overlap
Solvent Exposed Amides
Issue Date2002
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, 2002, v. 23 n. 4, p. 317-322 How to Cite?
AbstractThe recent introduction of the SEA-TROSY experiment (Pellecchia et al. (2001) J. Am. Chem. Soc., 123, 4633-4634) can alleviate the problem of resonance overlap in 15N/ 2H labeled proteins. This method selectively observes solvent exposed amide protons with a SEA element. However, SEA-TROSY spectra may be contaminated with exchange-relayed NOE contributions from fast exchanging hydroxyl or amine protons and longitudinal relaxation contributions. Furthermore, for non-deuterated proteins or protein-ligand complexes, SEA-TROSY spectra may contain NOE contributions from aliphatic protons. In this communication, a modified version of the SEA element, a Clean SEA element, is introduced to eliminate these artifacts.
Persistent Identifierhttp://hdl.handle.net/10722/157342
ISSN
2015 Impact Factor: 3.439
2015 SCImago Journal Rankings: 2.043
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorLin, Den_US
dc.contributor.authorSze, KHen_US
dc.contributor.authorCui, Yen_US
dc.contributor.authorZhu, Gen_US
dc.date.accessioned2012-08-08T08:49:04Z-
dc.date.available2012-08-08T08:49:04Z-
dc.date.issued2002en_US
dc.identifier.citationJournal Of Biomolecular Nmr, 2002, v. 23 n. 4, p. 317-322en_US
dc.identifier.issn0925-2738en_US
dc.identifier.urihttp://hdl.handle.net/10722/157342-
dc.description.abstractThe recent introduction of the SEA-TROSY experiment (Pellecchia et al. (2001) J. Am. Chem. Soc., 123, 4633-4634) can alleviate the problem of resonance overlap in 15N/ 2H labeled proteins. This method selectively observes solvent exposed amide protons with a SEA element. However, SEA-TROSY spectra may be contaminated with exchange-relayed NOE contributions from fast exchanging hydroxyl or amine protons and longitudinal relaxation contributions. Furthermore, for non-deuterated proteins or protein-ligand complexes, SEA-TROSY spectra may contain NOE contributions from aliphatic protons. In this communication, a modified version of the SEA element, a Clean SEA element, is introduced to eliminate these artifacts.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.subjectAmide Hydrogen Exchangeen_US
dc.subjectClean-Pmen_US
dc.subjectHsqcen_US
dc.subjectProteinsen_US
dc.subjectResonance Overlapen_US
dc.subjectSolvent Exposed Amidesen_US
dc.titleClean SEA-HSQC: A method to map solvent exposed amides in large non-deuterated proteins with gradient-enhanced HSQCen_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:1020225206644en_US
dc.identifier.scopuseid_2-s2.0-0036700882en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0036700882&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume23en_US
dc.identifier.issue4en_US
dc.identifier.spage317en_US
dc.identifier.epage322en_US
dc.identifier.isiWOS:000177984600007-
dc.publisher.placeNetherlandsen_US
dc.identifier.scopusauthoridLin, D=9036520900en_US
dc.identifier.scopusauthoridSze, KH=7006735061en_US
dc.identifier.scopusauthoridCui, Y=7402595461en_US
dc.identifier.scopusauthoridZhu, G=7402633110en_US

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