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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, Isabel
Alonso Hernández, José Luis
Año del Documento: 2015
Documento Fuente: Physical Chemistry Chemical Physics, 2015, 17, 20274-20280
Resumen: 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: info:eu-repo/semantics/restrictedAccess
Aparece en las colecciones:DEP63 - Artículos de revista



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