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dc.contributor.authorFaggi, Enrico
dc.contributor.authorLuis Lafuente, Santiago Vicente
dc.contributor.authorAlfonso Rodríguez, Ignacio
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.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

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