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dc.contributor.authorCabezas, Carlos
dc.contributor.authorRobben, Martinus A. T.
dc.contributor.authorRijs, Anouk M.
dc.contributor.authorPeña Calvo, María Isabel 
dc.contributor.authorAlonso Hernández, José Luis 
dc.date.accessioned2017-03-19T16:05:22Z
dc.date.available2017-03-19T16:05:22Z
dc.date.issued2015
dc.identifier.citationPhysical Chemistry Chemical Physics, 2015, 17, 20274-20280es
dc.identifier.urihttp://uvadoc.uva.es/handle/10324/22652
dc.description.abstractSerine capped dipeptide N-acetyl-L-serinamide (Ac-Ser-NH2) has been investigated using Fourier transform microwave spectroscopic techniques combined with laser ablation sources. Spectral signatures originating from one dominant species have been detected in the supersonic expansion. Rotational and nuclear quadrupole coupling constants of the two 14N nuclei have been used in the characterization of a Ceq/g-turn structure, which is stabilized by a C7O·· ·HN intramolecular hydrogen bond closing a seven-membered ring. Two extra hydrogen bonds involving the polar side chain (–CH2OH) further stabilize the structure. The non-observation of C5 species, attributed to the presence of the polar side chain, is in contrast with the previous gas phase observation of the related dipeptides containing glycine or alanine residues. The A–E splitting pattern arising from the internal rotation of the methyl group has been analyzed and the internal rotation barrier has been determined.es
dc.format.mimetypeapplication/pdfes
dc.language.isoenges
dc.rights.accessRightsinfo:eu-repo/semantics/restrictedAccesses
dc.titleFourier transform microwave spectroscopy of Ac-Ser-NH2: the role of side chain interactions in peptide foldinges
dc.typeinfo:eu-repo/semantics/articlees
dc.rights.holderOwner Societies 2015es
dc.identifier.doi10.1039/c5cp02654ges
dc.peerreviewedSIes


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