Minimalistic amino amides as models to study N–Hπ interactions and their implication in the side chain folding of pseudopeptidic molecules
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http://dx.doi.org/10.1039/C3RA41843J |
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Título
Minimalistic amino amides as models to study N–Hπ interactions and their implication in the side chain folding of pseudopeptidic moleculesFecha de publicación
2013Editor
Royal Society of ChemistryISSN
2046-2069Tipo de documento
info:eu-repo/semantics/articleVersión de la editorial
http://pubs.rsc.org/en/Content/ArticleLanding/2013/RA/c3ra41843j#!divAbstractResumen
The 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 ... [+]
The 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. [-]
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RSC Advances, 3Derechos de acceso
This journal is (c) The Royal Society of Chemistry 2013
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