Small angle X-ray scattering of wheat seed-storage proteins: α-, γ- and ω-gliadins and the high molecular weight (HMW) subunits of glutenin

Neil H. Thomson; Mervyn J. Miles; Yves Popineau; John Harries; Peter Shewry; Arthur S. Tatham

doi:10.1016/S0167-4838(99)00019-9

Small angle X-ray scattering of wheat seed-storage proteins: α-, γ- and ω-gliadins and the high molecular weight (HMW) subunits of glutenin

Neil H. Thomson, Mervyn J. Miles, Yves Popineau, John Harries, Peter Shewry, Arthur S. Tatham^*

^*Corresponding author for this work

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

71 Citations (Scopus)

Abstract

Small angle X-ray scattering in solution was performed on seed-storage proteins from wheat. Three different groups of gliadins (α-, γ- and ω-) and a high molecular weight (HMW) subunit of glutenin (1Bx20) were studied to determine molecular size parameters. All the gliadins could be modelled as prolate ellipsoids with extended conformations. The HMW subunit existed as a highly extended rod-like particle in solution with a length of about 69 nm and a diameter of about 6.4 nm. Specific aggregation effects were observed which may reflect mechanisms of self-assembly that contribute to the unique viscoelastic properties of wheat dough. Copyright (C) 1999 Elsevier Science B.V.

Original language	English
Pages (from-to)	359-366
Number of pages	8
Journal	Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Volume	1430
Issue number	2
DOIs	https://doi.org/10.1016/S0167-4838(99)00019-9
Publication status	Published - 19 Mar 1999
Externally published	Yes

Keywords

Gliadin
Glutenin
Small angle X-ray scattering

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10.1016/S0167-4838(99)00019-9

Cite this

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title = "Small angle X-ray scattering of wheat seed-storage proteins: α-, γ- and ω-gliadins and the high molecular weight (HMW) subunits of glutenin",

abstract = "Small angle X-ray scattering in solution was performed on seed-storage proteins from wheat. Three different groups of gliadins (α-, γ- and ω-) and a high molecular weight (HMW) subunit of glutenin (1Bx20) were studied to determine molecular size parameters. All the gliadins could be modelled as prolate ellipsoids with extended conformations. The HMW subunit existed as a highly extended rod-like particle in solution with a length of about 69 nm and a diameter of about 6.4 nm. Specific aggregation effects were observed which may reflect mechanisms of self-assembly that contribute to the unique viscoelastic properties of wheat dough. Copyright (C) 1999 Elsevier Science B.V.",

keywords = "Gliadin, Glutenin, Small angle X-ray scattering",

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year = "1999",

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doi = "10.1016/S0167-4838(99)00019-9",

language = "English",

volume = "1430",

pages = "359--366",

journal = "Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular",

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number = "2",

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Small angle X-ray scattering of wheat seed-storage proteins: α-, γ- and ω-gliadins and the high molecular weight (HMW) subunits of glutenin. / Thomson, Neil H.; Miles, Mervyn J.; Popineau, Yves et al.
In: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular, Vol. 1430, No. 2, 19.03.1999, p. 359-366.

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

TY - JOUR

T1 - Small angle X-ray scattering of wheat seed-storage proteins

T2 - α-, γ- and ω-gliadins and the high molecular weight (HMW) subunits of glutenin

AU - Thomson, Neil H.

AU - Miles, Mervyn J.

AU - Popineau, Yves

AU - Harries, John

AU - Shewry, Peter

AU - Tatham, Arthur S.

PY - 1999/3/19

Y1 - 1999/3/19

N2 - Small angle X-ray scattering in solution was performed on seed-storage proteins from wheat. Three different groups of gliadins (α-, γ- and ω-) and a high molecular weight (HMW) subunit of glutenin (1Bx20) were studied to determine molecular size parameters. All the gliadins could be modelled as prolate ellipsoids with extended conformations. The HMW subunit existed as a highly extended rod-like particle in solution with a length of about 69 nm and a diameter of about 6.4 nm. Specific aggregation effects were observed which may reflect mechanisms of self-assembly that contribute to the unique viscoelastic properties of wheat dough. Copyright (C) 1999 Elsevier Science B.V.

AB - Small angle X-ray scattering in solution was performed on seed-storage proteins from wheat. Three different groups of gliadins (α-, γ- and ω-) and a high molecular weight (HMW) subunit of glutenin (1Bx20) were studied to determine molecular size parameters. All the gliadins could be modelled as prolate ellipsoids with extended conformations. The HMW subunit existed as a highly extended rod-like particle in solution with a length of about 69 nm and a diameter of about 6.4 nm. Specific aggregation effects were observed which may reflect mechanisms of self-assembly that contribute to the unique viscoelastic properties of wheat dough. Copyright (C) 1999 Elsevier Science B.V.

KW - Gliadin

KW - Glutenin

KW - Small angle X-ray scattering

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DO - 10.1016/S0167-4838(99)00019-9

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VL - 1430

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JO - Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular

JF - Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular

IS - 2

ER -

Small angle X-ray scattering of wheat seed-storage proteins: α-, γ- and ω-gliadins and the high molecular weight (HMW) subunits of glutenin

Abstract

Keywords

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