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. 1991 Jan 1;88(1):68-71.
doi: 10.1073/pnas.88.1.68.

Scanning tunneling microscopy of a wheat seed storage protein reveals details of an unusual supersecondary structure

M J Miles  1 , H J Carr, T C McMaster, K J I'Anson, P S Belton, V J Morris, J M Field, P R Shewry, A S Tatham
Affiliations

Scanning tunneling microscopy of a wheat seed storage protein reveals details of an unusual supersecondary structure

M J Miles et al. Proc Natl Acad Sci U S A. .

Abstract

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.

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