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Please use this identifier to cite or link to this item: http://uvadoc.uva.es/handle/10324/22652
Title: Fourier transform microwave spectroscopy of Ac-Ser-NH2: the role of side chain interactions in peptide folding
Authors: Cabezas, Carlos
Robben, Martinus A. T.
Rijs, Anouk M.
Peña, Isabel
Alonso Hernández, José Luis
Issue Date: 2015
Citation: 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.
Peer Review: SI
DOI: 10.1039/c5cp02654g
Rights Owner: Owner Societies 2015
Language: eng
URI: http://uvadoc.uva.es/handle/10324/22652
Rights: info:eu-repo/semantics/restrictedAccess
Appears in Collections:DEP63 - Artículos de revista


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