Temperature-dependent intensity anomalies in amino acid esters: weak hydrogen bonds in protected glycine, alanine and valine

Temperature-dependent intensity anomalies in amino acid esters: weak hydrogen bonds in protected glycine, alanine and valine
Otto, K. E.; Hesse, S.; Wassermann, T. N.; Rice, C. A.; Suhm, M. A. ; Stafforst, T. & Diederichsen, U.  (2011) 
Physical Chemistry Chemical Physics13(31) pp. 14119-14130.​

Authors
Otto, Katharina E.; Hesse, Susanne; Wassermann, Tobias N.; Rice, Corey A.; Suhm, Martin A. ; Stafforst, Thorsten; Diederichsen, Ulf 
Issue Date
2011
Type
Journal Article
Publisher
Royal Soc Chemistry
Journal
Physical Chemistry Chemical Physics 
Organization
Institut für Physikalische Chemie 
ISSN
1463-9084; 1463-9076
Abstract
Esters of glycine, alanine and valine are investigated by FTIR and Raman spectroscopy in supersonic jets as gas phase model systems for the neutral peptide N-terminus. The NH-stretching vibrations exhibit very large temperature-and substitution-dependent intensity anomalies which are related to weak, bifurcated intramolecular hydrogen bonds to the carbonyl group. Comparison to theory is only satisfactory at low temperature. Spectral NH aggregation shifts are small or even negligible and the associated IR intensity is remarkably low. In the case of valine, chirality recognition effects are nevertheless detected and rationalized. Comparison to quantum-chemical calculations for dimers shows that dispersion interactions are essential. It also rules out cooperative hydrogen bond topologies and points at deficiencies in standard harmonic treatments with the linear dipole approximation.
Publication of Göttingen University
Yes
Sponsor
Funder: DFG [Su121/2]; Fonds der Chemischen Industrie
c1cp20883g_Otto.pdf3.51 MBAdobe PDF

Reference

Citations

20 citations in SCOPUS
22 citations in WoS

Social Media


Published version

Special user license Goescholar/GRO License