University of Illinois Urbana-Champaign

Preferred conformers of non-proteinogenic amino acids homoserine and homocysteine

Alonso, José L.

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1807.pdf
663169.pptx

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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.
Publisher
International Symposium on Molecular Spectroscopy
Type of Resource
text
Genre of Resource
Conference Paper / Presentation
Language
En
Permalink
http://hdl.handle.net/2142/91256
Copyright and License Information
Copyright 2016 by the authors

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Abstracts & Presentations - 2016 International Symposium on Molecular Spectroscopy PRIMARY