Ang, S., Kogulanathan, J., Morris, Gordon, Kök, M. S., Shewry, P. R., Tatham, A. S., Adams, G. G., Rowe, A. J. and Harding, S. E. (2010) Structure and heterogeneity of gliadin: A hydrodynamic evaluation. European Biophysics Journal, 39 (2). pp. 255-261. ISSN 0175-7571

This is the latest version of this item.


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. © 2009 European Biophysical Societies' Association.

Structure_and_heterogeneity_of_gliadin_a_hydrodynamic_evaluation.pdf - Accepted Version

Download (361kB) | Preview


Downloads per month over past year

Add to AnyAdd to TwitterAdd to FacebookAdd to LinkedinAdd to PinterestAdd to Email