Scanning tunneling microscopy of a wheat seed storage protein reveals details of an unusual supersecondary structure
1991
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.
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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