التفاصيل البيبلوغرافية
| العنوان: |
Wheat glutenin proteins assemble into a nanostructure with unusual structural features |
| المؤلفون: |
Mackintosh, Sarah H.1, Meade, Susie J.1, Healy, Jackie P.2, Sutton, Kevin H.1, Larsen, Nigel G.1, Squires, Adam M.3, Gerrard, Juliet A.2 juliet.gerrard@canterbury.ac.nz |
| المصدر: |
Journal of Cereal Science. Jan2009, Vol. 49 Issue 1, p157-162. 6p. |
| مصطلحات موضوعية: |
*PLANT proteins, *WHEAT, *NANOSTRUCTURES, *MOLECULAR weights, *MOLECULAR structure, *X-ray diffraction |
| مستخلص: |
Abstract: The 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 38.7Å) inconsistent with both the classic amyloid form and the previously described β-helix structure. The 4.6Å reflection is consistent with that predicted for the amyloid inter-β-strand, and the absence of the inter-β-sheet distance at ≈10–11Å 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. [Copyright &y& Elsevier] |
| قاعدة البيانات: |
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