2024-04-10T06:06:21Zhttps://uvadoc.uva.es/oai/requestoai:uvadoc.uva.es:10324/226522021-06-23T11:52:54Zcom_10324_1186com_10324_931com_10324_894col_10324_1404
2017-03-19T16:05:22Z
urn:hdl:10324/22652
Fourier transform microwave spectroscopy of Ac-Ser-NH2: the role of side chain interactions in peptide folding
Cabezas, Carlos
Robben, Martinus A. T.
Rijs, Anouk M.
Peña Calvo, María Isabel
Alonso Hernández, José Luis
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.
2017-03-19T16:05:22Z
2017-03-19T16:05:22Z
2015
info:eu-repo/semantics/article
Physical Chemistry Chemical Physics, 2015, 17, 20274-20280
http://uvadoc.uva.es/handle/10324/22652
10.1039/c5cp02654g
eng
info:eu-repo/semantics/restrictedAccess
Owner Societies 2015