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

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 seque...

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Veröffentlicht in:Proceedings of the National Academy of Sciences - PNAS 1991-01, Vol.89 (1), p.68-71
Hauptverfasser: Miles, MJ, Carr, HJ, McMaster, T C, I'Anson, K J, Belton, P S, Morris, V J, Field, J M, Shewry, PR, Tatham, A S
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Sprache:eng
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Zusammenfassung: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.
ISSN:0027-8424