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Article: The use of a ditopic Gd(III) paramagnetic probe for investigating α-bungarotoxin surface accessibility

TitleThe use of a ditopic Gd(III) paramagnetic probe for investigating α-bungarotoxin surface accessibility
Authors
KeywordsGd(III) complexes
NMR spectroscopy
Paramagnetic probe
Protein hydration
Protein surface accessibility
Issue Date2012
PublisherElsevier Inc. The Journal's web site is located at http://www.elsevier.com/locate/jinorgbio
Citation
Journal Of Inorganic Biochemistry, 2012, v. 112, p. 25-31 How to Cite?
AbstractProtein surface accessibility is a critical parameter which drives all intermolecular interaction processes. In this respect a big deal of information has been derived by analyzing paramagnetic perturbation profiles obtained from NMR protein spectra, particularly in the case that the effects due to different soluble paramagnets can be compared. Here Gd 2L7, a neutral ditopic paramagnetic NMR probe, has been characterized in terms of structure and relaxivity and its paramagnetic perturbations on α-bungarotoxin CαH signals in 1H- 13C HSQC (heteronuclear single quantum coherence) spectra have been analyzed. Then, these signal attenuations have been compared with the ones previously obtained in the presence of GdDTPA-BMA (gadolinium(III) diethylenetriamine-N,N,N′,N'″,N″- pentaacetate-bis(methylamide)). In spite of the different molecular size and shape, for the two probes a common pathway of approach to the α-bungarotoxin surface can be observed with an equally enhanced access of both GdDTPA-BMA and Gd 2L7 toward the protein surface side where residues involved in the receptor binding are located. The different residence times of the water molecule directly coordinated by the Gd(III) ion measured for the two paramagnets account for the reduced broadening of water signal in the presence of the ditopic probe at equivalent gadolinium concentration. These features make Gd 2L7 a very suitable probe for investigating protein surface accessibility of complex protein systems. © 2012 Elsevier Inc.
Persistent Identifierhttp://hdl.handle.net/10722/152640
ISSN
2014 Impact Factor: 3.444
2014 SCImago Journal Rankings: 0.849
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorBernini, Aen_HK
dc.contributor.authorSpiga, Oen_HK
dc.contributor.authorVenditti, Ven_HK
dc.contributor.authorPrischi, Fen_HK
dc.contributor.authorBotta, Men_HK
dc.contributor.authorCroce, Gen_HK
dc.contributor.authorTong, APLen_HK
dc.contributor.authorWong, WTen_HK
dc.contributor.authorNiccolai, Nen_HK
dc.date.accessioned2012-07-16T09:44:48Z-
dc.date.available2012-07-16T09:44:48Z-
dc.date.issued2012en_HK
dc.identifier.citationJournal Of Inorganic Biochemistry, 2012, v. 112, p. 25-31en_HK
dc.identifier.issn0162-0134en_HK
dc.identifier.urihttp://hdl.handle.net/10722/152640-
dc.description.abstractProtein surface accessibility is a critical parameter which drives all intermolecular interaction processes. In this respect a big deal of information has been derived by analyzing paramagnetic perturbation profiles obtained from NMR protein spectra, particularly in the case that the effects due to different soluble paramagnets can be compared. Here Gd 2L7, a neutral ditopic paramagnetic NMR probe, has been characterized in terms of structure and relaxivity and its paramagnetic perturbations on α-bungarotoxin CαH signals in 1H- 13C HSQC (heteronuclear single quantum coherence) spectra have been analyzed. Then, these signal attenuations have been compared with the ones previously obtained in the presence of GdDTPA-BMA (gadolinium(III) diethylenetriamine-N,N,N′,N'″,N″- pentaacetate-bis(methylamide)). In spite of the different molecular size and shape, for the two probes a common pathway of approach to the α-bungarotoxin surface can be observed with an equally enhanced access of both GdDTPA-BMA and Gd 2L7 toward the protein surface side where residues involved in the receptor binding are located. The different residence times of the water molecule directly coordinated by the Gd(III) ion measured for the two paramagnets account for the reduced broadening of water signal in the presence of the ditopic probe at equivalent gadolinium concentration. These features make Gd 2L7 a very suitable probe for investigating protein surface accessibility of complex protein systems. © 2012 Elsevier Inc.en_HK
dc.languageengen_US
dc.publisherElsevier Inc. The Journal's web site is located at http://www.elsevier.com/locate/jinorgbioen_HK
dc.relation.ispartofJournal of Inorganic Biochemistryen_HK
dc.subjectGd(III) complexesen_HK
dc.subjectNMR spectroscopyen_HK
dc.subjectParamagnetic probeen_HK
dc.subjectProtein hydrationen_HK
dc.subjectProtein surface accessibilityen_HK
dc.titleThe use of a ditopic Gd(III) paramagnetic probe for investigating α-bungarotoxin surface accessibilityen_HK
dc.typeArticleen_HK
dc.identifier.emailWong, WT: wtwong@hku.hken_HK
dc.identifier.authorityWong, WT=rp00811en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.jinorgbio.2012.03.004en_HK
dc.identifier.pmid22542593-
dc.identifier.scopuseid_2-s2.0-84860224515en_HK
dc.identifier.hkuros201419en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-84860224515&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume112en_HK
dc.identifier.spage25en_HK
dc.identifier.epage31en_HK
dc.identifier.isiWOS:000305501300004-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridBernini, A=7004103621en_HK
dc.identifier.scopusauthoridSpiga, O=6603012863en_HK
dc.identifier.scopusauthoridVenditti, V=8560856700en_HK
dc.identifier.scopusauthoridPrischi, F=6505683929en_HK
dc.identifier.scopusauthoridBotta, M=22955486900en_HK
dc.identifier.scopusauthoridCroce, G=7005670668en_HK
dc.identifier.scopusauthoridTong, APL=36547010300en_HK
dc.identifier.scopusauthoridWong, WT=7403973084en_HK
dc.identifier.scopusauthoridNiccolai, N=7003440494en_HK
dc.identifier.citeulike10493039-

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