Preferred conformers of non-proteinogenic amino acids homoserine and homocysteine
Alonso, José L.
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https://hdl.handle.net/2142/91256
Description
Title
Preferred conformers of non-proteinogenic amino acids homoserine and homocysteine
Author(s)
Alonso, José L.
Contributor(s)
Cabezas, Carlos
Alonso, E. R.
Mata, Santiago
Rodríguez, Miguel A.
Díez, Verónica
Issue Date
2016-06-22
Keyword(s)
Chirped pulse
Date of Ingest
2017-01-26T21:37:40Z
Abstract
Vaporization of solid homoserine and homocysteine by laser ablation in combination with Fourier transform microwave spectroscopy techniques made possible the detection of their most stable structures in a supersonic expansion. All detected conformers have been identified through their rotational and $^{14}$N quadrupole coupling constants. They show hydrogen bonds linking the amino and carboxylic group through N--H$\cdot\cdot\cdot$O=C (type I) or N$\cdot\cdot\cdot$H--O (type II) interactions. In some of them there are additional hydrogen bonds established between the amino group and the hydroxyl/thiol groups in the gamma position. Entropic effects related to the side chain have been found to be significant in determining the most populated conformations.
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