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Secondary structure analysis of barley aleurone holoprotein by FTIR spectroscopy

I. BRATU1,* , M. TOMOAIA-COTISEL2, G. DAMIAN3, A. MOCANU2

Affiliation

  1. National Institute for R&D of Isotopic and Molecular Technology, P.O. Box 700, RO-400293 Cluj-Napoca, Romania
  2. ”Babes-Bolyai” University, Faculty of Chemistry, 11 Arany Janos st, Cluj-Napoca, Romania
  3. Babes-Bolyai” University, Faculty of Physics, 1 Kogalniceanu st, Cluj-Napoca, Romania

Abstract

Structural information of barley aleurone at various temperatures is obtained by analysis of the conformationally-sensitive amide I band using FT-IR spectroscopy. The second derivative spectrum was performed in order to overcome the bands overlapping due to the different C=O stretching vibrations of each type of secondary structure (i.e. α-helix, β-sheet, turns and unordered). The results of quantitative analysis by curve fitting to the inverted second derivative spectra indicate perturbations of both α-helix and β-sheet structures in thermal unfolding process, depending on the temperature values..

Keywords

FTIR spectroscopy, Secondary structure, Proteins, Barley aleurone, Deconvolution.

Submitted at: Nov. 15, 2006
Accepted at: March 15, 2007

Citation

I. BRATU, M. TOMOAIA-COTISEL, G. DAMIAN, A. MOCANU, Secondary structure analysis of barley aleurone holoprotein by FTIR spectroscopy, Journal of Optoelectronics and Advanced Materials Vol. 9, Iss. 3, pp. 672-674 (2007)