%0 Journal Article
%T Ab-Initio calculations of proline vibrations with and without water, consequences on the infrared spectra of proline-rich proteins
%+ Centre de recherches Paul Pascal (CRPP)
%+ Laboratoire Charles Coulomb (L2C)
%+ Université Sciences et Technologies - Bordeaux 1 (UB)
%+ Chimie et Biologie des Membranes et des Nanoobjets (CBMN)
%+ Laboratoire de Physico-Chimie Moléculaire (LPCM)
%A Banc, Amélie
%A Desbat, Bernard
%A Cavagnat, D.
%< avec comité de lecture
%@ 0003-7028
%J Applied Spectroscopy
%I Society for Applied Spectroscopy
%V 65
%N 7
%P 817-819
%8 2011-07-01
%D 2011
%R 10.1366/11-06284
%K ab-initio calculations
%K prolines
%K vibration mode
%K gliadins
%Z Chemical Sciences/Theoretical and/or physical chemistryJournal articles
%X The infrared spectra of proline rich proteins display a strong band in the 1450 cm-1 region. In the literature, this band was assigned either to the deformation modes of the CH2 and CH3 groups or to the CN stretching mode of proline residues. In order to establish the correct assignment of this band, the impact of proline vibrations in a polypeptide chain is studied and ab-initio calculations are performed for a model molecule (I) containing a repeat unit of polyproline. A strong band is effectively calculated in the 1450 cm-1 region and mostly assigned to CN stretching whereas, due to the absence of N-H bond, there is no amide II band. These results are in good agreement with the spectral features observed in the FTIR spectra of gliadins. Moreover, the spectral shifts calculated when a water molecule is complexed with (I) are consistent with the hydration effect observed in the experimental data.
%G English
%2 https://hal.science/hal-00627738/document
%2 https://hal.science/hal-00627738/file/Applied_Spectroscopy.pdf
%L hal-00627738
%U https://hal.science/hal-00627738
%~ CNRS
%~ CRPP
%~ L2C
%~ INC-CNRS
%~ MIPS
%~ UNIV-MONTPELLIER
%~ UM-2015-2021