Structure and heterogeneity of gliadin: a hydrodynamic evaluation

Ang, S., Kogulanathan, J., Morris, G. A., Kok, M. S., Shewry, Peter, Tatham, A. S., Adams, G. G., Rowe, A. J. and Harding, S. E. (2009) Structure and heterogeneity of gliadin: a hydrodynamic evaluation. European Biophysics Journal, 39 (Januar). pp. 255-261. 10.1007/s00249-009-0529-7
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A study of the heterogeneity and conformation in solution [in 70% (v/v) aq. ethanol] of gliadin proteins from wheat was undertaken based upon sedimentation velocity in the analytical ultracentrifuge, analysis of the distribution coefficients and ellipsoidal axial ratios assuming quasi-rigid particles, allowing for a range of plausible time-averaged hydration values. All classical fractions (α, γ, ωslow, ωfast) show three clearly resolved components. Based on the weight-average sedimentation coefficient for each fraction and a weight-average molecular weight from sedimentation equilibrium and/or cDNA sequence analysis, all the proteins are extended molecules with axial ratios ranging from ~10 to 30 with α appearing the most extended and γ the least.
Item Type Article
Open Access Green
Keywords Gliadin , Sedimentation coefficient, Molecular weight, Heterogeneity, Axial ratio, Extended conformation
Project Centre for Crop Genetic Improvement (CGI), Cereal seed composition and end use quality
Date Deposited 05 Dec 2025 09:42
Last Modified 19 Dec 2025 14:31

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