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

doi:10.1007/s00249-009-0529-7

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

Cardiff School of Sport and Health Sciences

Research output: Contribution to journal › Article › peer-review

41 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, ω_slow, ω_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 ~10 to 30 with α appearing the most extended and γ the least.

Original language	English
Pages (from-to)	255-261
Number of pages	7
Journal	European Biophysics Journal
Volume	39
Issue number	2
DOIs	https://doi.org/10.1007/s00249-009-0529-7
Publication status	Published - 8 Aug 2009

Keywords

Axial ratio
Extended conformation
Gliadin
Heterogeneity
Molecular weight
Sedimentation coefficient

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10.1007/s00249-009-0529-7

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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.",

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AU - Kogulanathan, Jana

AU - Morris, Gordon A.

AU - Kök, M. Samil

AU - Shewry, Peter R.

AU - Tatham, Arthur S.

AU - Adams, Gary G.

AU - Rowe, Arthur J.

AU - Harding, Stephen E.

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Structure and heterogeneity of gliadin: A hydrodynamic evaluation

Abstract

Keywords

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