Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/5075
DC FieldValueLanguage
dc.contributor.authorStanczak, P.en_us
dc.contributor.authorValensin, Danielaen_us
dc.contributor.authorJuszczyk, P.en_us
dc.contributor.authorGrzonka, Z.en_us
dc.contributor.authorValensin, Giannien_us
dc.contributor.authorBernardi, F.en_us
dc.contributor.authorMolteni, E.en_us
dc.contributor.authorGaggelli, Elenaen_us
dc.contributor.authorKozlowski, H.en_us
dc.date.accessioned2021-03-30T15:48:51Z-
dc.date.available2021-03-30T15:48:51Z-
dc.date.issued2005-
dc.identifier.issn1359-7345en_US
dc.identifier.urihttp://hdl.handle.net/20.500.12779/5075-
dc.description27195en_US
dc.description.abstractThe interaction between the single hexarepeat unit of chicken prion protein [ChPrP(54–59)] and Cu(II) was investigated by NMR, finding different coordination modes for the trans/trans and cis/trans isomers.en_US
dc.language.isoenen_US
dc.relationNoneen_US
dc.relation.ispartofCHEMICAL COMMUNICATIONSen_US
dc.titleFine tuning the structure of the Cu2+ complex with the prion protein chicken repeat by proline isomerizationen_US
dc.typeArticleen_US
dc.identifier.doi10.1039/b504986een_US
dc.identifier.scopus2-s2.0-22544439356en_US
dc.identifier.isiWOS:000230117400015en_US
dc.relation.volume26en_US
dc.description.firstpage3298en_US
dc.description.lastpage3300en_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.orcid0000-0003-4187-3919-
crisitem.author.orcid9810-
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