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

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.