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Structure and heterogeneity of gliadin: a hydrodynamic evaluation
(Springer, 2010) Ang, Shirley; Kogulanathan, Jana; Morris, Gordon A.; Kök, Mehmet Şamil; Shewry, Peter R.
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 (alpha, gamma, omega(slow), omega(fast)) 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 similar to 10 to 30 with alpha appearing the most extended and gamma the least.