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Article: The use of a ditopic Gd(III) paramagnetic probe for investigating α-bungarotoxin surface accessibility
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TitleThe use of a ditopic Gd(III) paramagnetic probe for investigating α-bungarotoxin surface accessibility
 
AuthorsBernini, A4
Spiga, O5 4
Venditti, V6
Prischi, F3
Botta, M1
Croce, G1
Tong, APL2
Wong, WT2
Niccolai, N5 4
 
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
 
CitationJournal Of Inorganic Biochemistry, 2012, v. 112, p. 25-31 [How to Cite?]
DOI: http://dx.doi.org/10.1016/j.jinorgbio.2012.03.004
 
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.
 
ISSN0162-0134
2013 Impact Factor: 3.274
2013 SCImago Journal Rankings: 0.960
 
DOIhttp://dx.doi.org/10.1016/j.jinorgbio.2012.03.004
 
ISI Accession Number IDWOS:000305501300004
 
ReferencesReferences in Scopus
 
DC FieldValue
dc.contributor.authorBernini, A
 
dc.contributor.authorSpiga, O
 
dc.contributor.authorVenditti, V
 
dc.contributor.authorPrischi, F
 
dc.contributor.authorBotta, M
 
dc.contributor.authorCroce, G
 
dc.contributor.authorTong, APL
 
dc.contributor.authorWong, WT
 
dc.contributor.authorNiccolai, N
 
dc.date.accessioned2012-07-16T09:44:48Z
 
dc.date.available2012-07-16T09:44:48Z
 
dc.date.issued2012
 
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.
 
dc.description.naturelink_to_subscribed_fulltext
 
dc.identifier.citationJournal Of Inorganic Biochemistry, 2012, v. 112, p. 25-31 [How to Cite?]
DOI: http://dx.doi.org/10.1016/j.jinorgbio.2012.03.004
 
dc.identifier.citeulike10493039
 
dc.identifier.doihttp://dx.doi.org/10.1016/j.jinorgbio.2012.03.004
 
dc.identifier.epage31
 
dc.identifier.hkuros201419
 
dc.identifier.isiWOS:000305501300004
 
dc.identifier.issn0162-0134
2013 Impact Factor: 3.274
2013 SCImago Journal Rankings: 0.960
 
dc.identifier.pmid22542593
 
dc.identifier.scopuseid_2-s2.0-84860224515
 
dc.identifier.spage25
 
dc.identifier.urihttp://hdl.handle.net/10722/152640
 
dc.identifier.volume112
 
dc.languageeng
 
dc.publisherElsevier Inc. The Journal's web site is located at http://www.elsevier.com/locate/jinorgbio
 
dc.publisher.placeUnited States
 
dc.relation.ispartofJournal of Inorganic Biochemistry
 
dc.relation.referencesReferences in Scopus
 
dc.subjectGd(III) complexes
 
dc.subjectNMR spectroscopy
 
dc.subjectParamagnetic probe
 
dc.subjectProtein hydration
 
dc.subjectProtein surface accessibility
 
dc.titleThe use of a ditopic Gd(III) paramagnetic probe for investigating α-bungarotoxin surface accessibility
 
dc.typeArticle
 
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<contributor.author>Croce, G</contributor.author>
<contributor.author>Tong, APL</contributor.author>
<contributor.author>Wong, WT</contributor.author>
<contributor.author>Niccolai, N</contributor.author>
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Author Affiliations
  1. Università degli Studi del Piemonte Orientale Amedeo Avogadro, Alessandria
  2. The University of Hong Kong
  3. Imperial College London
  4. Università degli Studi di Siena
  5. SienaBioGrafix Srl
  6. National Institutes of Health, Bethesda