Abstract
Dipeptide L-threonyl-L-methionine (Thr-Met) is characterized structurally by means of a solid-state linear polarized IR- spectroscopy (IR-LD) of oriented samples as a colloidal suspension in nematic liquid crystal and quantum chemical ab initio calculations. Vibrational analysis supports the experimental data as well. The role of intermolecular hydrogen bonding on conformational behavior and spectroscopic properties of the compound, studied in solid state is determined.
Keywords: Thr-Met, IR-LD spectroscopy, ab initio calculations, solid-state
Protein & Peptide Letters
Title: Structural and IR-Spectroscopic Elucidation of Dipeptide L-Threonyl-LMethionine in Solid State
Volume: 16 Issue: 11
Author(s): A. G. Chapkanov and S. Y. Zareva
Affiliation:
Keywords: Thr-Met, IR-LD spectroscopy, ab initio calculations, solid-state
Abstract: Dipeptide L-threonyl-L-methionine (Thr-Met) is characterized structurally by means of a solid-state linear polarized IR- spectroscopy (IR-LD) of oriented samples as a colloidal suspension in nematic liquid crystal and quantum chemical ab initio calculations. Vibrational analysis supports the experimental data as well. The role of intermolecular hydrogen bonding on conformational behavior and spectroscopic properties of the compound, studied in solid state is determined.
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Cite this article as:
Chapkanov G. A. and Zareva Y. S., Structural and IR-Spectroscopic Elucidation of Dipeptide L-Threonyl-LMethionine in Solid State, Protein & Peptide Letters 2009; 16 (11) . https://dx.doi.org/10.2174/092986609789353628
DOI https://dx.doi.org/10.2174/092986609789353628 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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