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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35 Citations (Scopus)

Abstract

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
Volume39
Issue number2
Early online date8 Aug 2009
DOIs
Publication statusPublished - Jan 2010
Externally publishedYes

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    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. https://doi.org/10.1007/s00249-009-0529-7