Structure and heterogeneity of gliadin: A hydrodynamic evaluation

Shirley Ang, Jana Kogulanathan, Gordon A. Morris, M. Samil Kök, Peter R. Shewry, Arthur S. Tatham, Gary G. Adams, Arthur J. Rowe, Stephen E. Harding

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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.

Original languageEnglish
Pages (from-to)255-261
Number of pages7
JournalEuropean Biophysics Journal
Issue number2
Early online date8 Aug 2009
Publication statusPublished - Jan 2010
Externally publishedYes


Cite this

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