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    • Dpto. Química Física y Química Inorgánica
    • DEP63 - Artículos de revista
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    Por favor, use este identificador para citar o enlazar este ítem:http://uvadoc.uva.es/handle/10324/22652

    Título
    Fourier transform microwave spectroscopy of Ac-Ser-NH2: the role of side chain interactions in peptide folding
    Autor
    Cabezas, Carlos
    Robben, Martinus A. T.
    Rijs, Anouk M.
    Peña Calvo, María IsabelAutoridad UVA
    Alonso Hernández, José LuisAutoridad UVA Orcid
    Año del Documento
    2015
    Documento Fuente
    Physical Chemistry Chemical Physics, 2015, 17, 20274-20280
    Abstract
    Serine 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.
    Revisión por pares
    SI
    DOI
    10.1039/c5cp02654g
    Propietario de los Derechos
    Owner Societies 2015
    Idioma
    eng
    URI
    http://uvadoc.uva.es/handle/10324/22652
    Derechos
    restrictedAccess
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    • DEP63 - Artículos de revista [223]
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