Wheat glutenin proteins assemble into a nanostructure with unusual structural featuresMackintosh, S.H., Meade, S.J., Healy, J.P., Sutton, K.H., Larsen, N.G., Squires, A.M. and Gerrard, J.A. (2009) Wheat glutenin proteins assemble into a nanostructure with unusual structural features. Journal of Cereal Science, 49 (1). pp. 157-162. ISSN 0733-5210 Full text not archived in this repository. It is advisable to refer to the publisher's version if you intend to cite from this work. See Guidance on citing. To link to this item DOI: 10.1016/j.jcs.2008.08.003 Abstract/SummaryThe proteins of wheat have a known propensity to aggregate into a variety of forms. We report here a novel nanostructure from wheat proteins, derived from a crude extract of high molecular weight glutenins. The structure was characterised by a significant thioflavin T (ThT) fluorescence and a fibrillar morphology by transmission electron microscopy (TEM). The ThT fluorescence and TEM data are suggestive of an amyloid structure, but the X-ray fibre diffraction data show a reflection pattern (4.02, 4.2-4.3, 4.6, 12.9,19.3 and 38.7 angstrom) inconsistent with both the classic amyloid form and the previously described beta-helix structure. The 4.6 angstrom reflection is consistent with that predicted for the amyloid inter-beta-strand, and the absence of the inter-beta-sheet distance at approximate to 10-11 angstrom is not unprecedented in amyloid-like structures. However, our observed X-ray reflection pattern has not been previously reported and suggests a novel wheat glutenin nanostructure. (C) 2008 Elsevier Ltd. All rights reserved.
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