Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/6112
DC FieldValueLanguage
dc.contributor.authorBernini, Andreaen_us
dc.contributor.authorVenditti, V.en_us
dc.contributor.authorPrischi, F.en_us
dc.contributor.authorBotta, Maurizioen_us
dc.contributor.authorCroce, G.en_us
dc.contributor.authorTong, A. P. L.en_us
dc.contributor.authorWong, W. T.en_us
dc.contributor.authorNiccolai, Nerien_us
dc.date.accessioned2021-03-30T15:59:45Z-
dc.date.available2021-03-30T15:59:45Z-
dc.date.issued2012-
dc.identifier.issn0162-0134en_US
dc.identifier.urihttp://hdl.handle.net/20.500.12779/6112-
dc.description47141en_US
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(2)L7, 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 ((1))H-((13))C 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(2)L7 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(2)L7 a very suitable probe for investigating protein surface accessibility of complex protein systems.en_US
dc.language.isoenen_US
dc.relationNoneen_US
dc.relation.ispartofJOURNAL OF INORGANIC BIOCHEMISTRYen_US
dc.titleThe use of a ditopic Gd(III) paramagnetic probe for investigating α-bungarotoxin surface accessibility.en_US
dc.typeArticleen_US
dc.identifier.doi10.1016/j.jinorgbio.2012.03.004en_US
dc.identifier.pmid22542593en_US
dc.identifier.scopus2-s2.0-84860224515en_US
dc.identifier.isiWOS:000305501300004en_US
dc.identifier.urlhttp://linkinghub.elsevier.com/retrieve/pii/S0162-0134(12)00083-9en_US
dc.relation.volume112en_US
dc.description.firstpage25en_US
dc.description.lastpage31en_US
dc.description.thirdmissionNot applicableen_US
item.cerifentitytypePublications-
item.grantfulltextnone-
item.languageiso639-1en-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.openairetypeArticle-
item.fulltextNo Fulltext-
crisitem.author.orcid0000-0002-7528-2749-
crisitem.author.orcid0000-0003-0456-6995-
crisitem.author.orcid0000-0002-6919-6908-
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