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Structure and heterogeneity of gliadin: A hydrodynamic evaluation

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

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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. © 2009 European Biophysical Societies' Association.

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Item Type: Article
Uncontrolled Keywords: Axial ratio Extended conformation Gliadin Heterogeneity Molecular weight Sedimentation coefficient Algorithms Genetic Heterogeneity Motion Protein Conformation Sequence Analysis, DNA Time Factors Triticum Ultracentrifugation Water Triticum aestivum
Subjects: Q Science > QD Chemistry
Schools: School of Applied Sciences
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Depositing User: Gordon Morris
Date Deposited: 18 Sep 2012 13:17
Last Modified: 28 Aug 2021 20:32

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