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dc.contributor.authorFaggi, Enrico
dc.contributor.authorLuis Lafuente, Santiago Vicente
dc.contributor.authorAlfonso Rodríguez, Ignacio
dc.date.accessioned2015-02-26T12:56:51Z
dc.date.available2015-02-26T12:56:51Z
dc.date.issued2013
dc.identifier.issn2046-2069
dc.identifier.urihttp://hdl.handle.net/10234/115063
dc.description.abstractThe structural study of simple amino amides derived from natural amino acids showed a unique conformational pattern for the aromatic residues, being clearly different from that for the aliphatic derivatives. The results from a detailed NMR analysis, supported by DFT calculations, indicate that the aromatic side chain tends to fold over the amino amide moiety, involving a stabilizing polar N–Hπ interaction. The implications of this folding in the establishing of non-covalent interactions is also discussed.ca_CA
dc.format.extent10 p.ca_CA
dc.format.mimetypeapplication/pdfca_CA
dc.language.isoengca_CA
dc.publisherRoyal Society of Chemistryca_CA
dc.relation.isPartOfRSC Advances, 3ca_CA
dc.rightsThis journal is (c) The Royal Society of Chemistry 2013ca_CA
dc.titleMinimalistic amino amides as models to study N–Hπ interactions and their implication in the side chain folding of pseudopeptidic moleculesca_CA
dc.typeinfo:eu-repo/semantics/articleca_CA
dc.identifier.doihttp://dx.doi.org/10.1039/C3RA41843J
dc.rights.accessRightsinfo:eu-repo/semantics/restrictedAccessca_CA
dc.relation.publisherVersionhttp://pubs.rsc.org/en/Content/ArticleLanding/2013/RA/c3ra41843j#!divAbstractca_CA


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