对一种小麦种子贮藏蛋白进行扫描隧道显微镜观察，揭示了一种不同寻常的超二级结构的细节。
Scanning tunneling microscopy of a wheat seed storage protein reveals details of an unusual supersecondary structure.
作者信息
Miles M J, Carr H J, McMaster T C, I'Anson K J, Belton P S, Morris V J, Field J M, Shewry P R, Tatham A S
机构信息
Agricultural and Food Research Council, Institute of Food Research, Norwich, United Kingdom.
出版信息
Proc Natl Acad Sci U S A. 1991 Jan 1;88(1):68-71. doi: 10.1073/pnas.88.1.68.
Scanning tunneling microscopy has been used to demonstrate that a spiral structure based on beta-reverse turns is adopted by the repeat sequences present in a group of wheat gluten proteins. This structure is similar to the beta-spiral formed by a synthetic polypentapeptide based on a repeat sequence present in elastin. Wheat gluten and elastin are both elastomeric and it is possible that the spiral structure contributes to this property.
扫描隧道显微镜已被用于证明，一组小麦面筋蛋白中存在的重复序列采用了基于β-反向转角的螺旋结构。这种结构类似于由基于弹性蛋白中存在的重复序列的合成聚五肽形成的β-螺旋。小麦面筋和弹性蛋白都是弹性体，螺旋结构可能有助于这种特性。
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