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Article: NMR studies of lysozyme surface accessibility by using different paramagnetic relaxation probes

TitleNMR studies of lysozyme surface accessibility by using different paramagnetic relaxation probes
Authors
Issue Date2006
PublisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journals/jacsat/index.html
Citation
Journal Of The American Chemical Society, 2006, v. 128 n. 29, p. 9290-9291 How to Cite?
AbstractParamagnetic probes, whose approach to proteins can be monitored by nuclear magnetic resonance (NMR) studies, have been found to be of primary relevance for investigating protein surfaces' accessibility. Here, a Gd(III) neutral complex which contains two metal ions, [Gd2(L7)(H2O)2], is suggested as a paramagnetic probe particularly suited for systematic NMR investigation of protein surface accessibility, due to an expected high relaxivity and to the lack of electric charge which could favor specific interactions. Hen egg white lysozyme has been used as a model system to verify the absence of preferential approaches of this paramagnetic probe to specific protein moieties by comparing paramagnetic perturbation profiles of1H-13C HSQC signals obtained in the presence of TEMPOL and [Gd2(L7)(H2O)2]. From the similarity of the measured paramagnetic perturbation profiles induced by the two different probes, specific interactions of [Gd2(L7)(H2O)2]with the enzyme could be ruled out. The large size of the latter probe is suggested to be responsible for the strong paramagnetic perturbations observed for CαH groups which are located in convex surface-exposed regions. The combined use of the two probes reveals fine details of the dynamics controlling their approach toward the protein surface. Copyright © 2006 American Chemical Society.
Persistent Identifierhttp://hdl.handle.net/10722/70054
ISSN
2015 Impact Factor: 13.038
2015 SCImago Journal Rankings: 7.123
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.authorBracci, Len_HK
dc.contributor.authorTong, APLen_HK
dc.contributor.authorWong, WTen_HK
dc.contributor.authorNiccolai, Nen_HK
dc.date.accessioned2010-09-06T06:19:17Z-
dc.date.available2010-09-06T06:19:17Z-
dc.date.issued2006en_HK
dc.identifier.citationJournal Of The American Chemical Society, 2006, v. 128 n. 29, p. 9290-9291en_HK
dc.identifier.issn0002-7863en_HK
dc.identifier.urihttp://hdl.handle.net/10722/70054-
dc.description.abstractParamagnetic probes, whose approach to proteins can be monitored by nuclear magnetic resonance (NMR) studies, have been found to be of primary relevance for investigating protein surfaces' accessibility. Here, a Gd(III) neutral complex which contains two metal ions, [Gd2(L7)(H2O)2], is suggested as a paramagnetic probe particularly suited for systematic NMR investigation of protein surface accessibility, due to an expected high relaxivity and to the lack of electric charge which could favor specific interactions. Hen egg white lysozyme has been used as a model system to verify the absence of preferential approaches of this paramagnetic probe to specific protein moieties by comparing paramagnetic perturbation profiles of1H-13C HSQC signals obtained in the presence of TEMPOL and [Gd2(L7)(H2O)2]. From the similarity of the measured paramagnetic perturbation profiles induced by the two different probes, specific interactions of [Gd2(L7)(H2O)2]with the enzyme could be ruled out. The large size of the latter probe is suggested to be responsible for the strong paramagnetic perturbations observed for CαH groups which are located in convex surface-exposed regions. The combined use of the two probes reveals fine details of the dynamics controlling their approach toward the protein surface. Copyright © 2006 American Chemical Society.en_HK
dc.languageengen_HK
dc.publisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journals/jacsat/index.htmlen_HK
dc.relation.ispartofJournal of the American Chemical Societyen_HK
dc.titleNMR studies of lysozyme surface accessibility by using different paramagnetic relaxation probesen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0002-7863&volume=128&spage=9290&epage=9291&date=2006&atitle=NMR+Studies+of+Lysozyme+Surface+Accessibility+by+Using+Different+Paramagnetic+Relaxation+Probes+en_HK
dc.identifier.emailWong, WT: wtwong@hku.hken_HK
dc.identifier.authorityWong, WT=rp00811en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1021/ja062109yen_HK
dc.identifier.pmid16848438-
dc.identifier.scopuseid_2-s2.0-33746344709en_HK
dc.identifier.hkuros127620en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-33746344709&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume128en_HK
dc.identifier.issue29en_HK
dc.identifier.spage9290en_HK
dc.identifier.epage9291en_HK
dc.identifier.isiWOS:000239120700016-
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.scopusauthoridBracci, L=7006252899en_HK
dc.identifier.scopusauthoridTong, APL=36547010300en_HK
dc.identifier.scopusauthoridWong, WT=7403973084en_HK
dc.identifier.scopusauthoridNiccolai, N=7003440494en_HK
dc.identifier.citeulike4521898-

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