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Issue 31, 2015
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Fourier transform microwave spectroscopy of Ac-Ser-NH2: the role of side chain interactions in peptide folding

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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 Ceq7/γ-turn structure, which is stabilized by a CO⋯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.

Graphical abstract: Fourier transform microwave spectroscopy of Ac-Ser-NH2: the role of side chain interactions in peptide folding

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Supplementary files

Article information


Submitted
07 May 2015
Accepted
01 Jul 2015
First published
01 Jul 2015

Phys. Chem. Chem. Phys., 2015,17, 20274-20280
Article type
Paper
Author version available

Fourier transform microwave spectroscopy of Ac-Ser-NH2: the role of side chain interactions in peptide folding

C. Cabezas, M. A. T. Robben, A. M. Rijs, I. Peña and J. L. Alonso, Phys. Chem. Chem. Phys., 2015, 17, 20274
DOI: 10.1039/C5CP02654G

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