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

Mervyn J. Miles; Helen J. Carr; Terence C. Mcmaster; Kenneth J. I'Anson; Peter S. Belton; Victor J. Morris; J. Michael Field; Peter R. Shewry; Arthur S. Tatham

doi:10.1073/pnas.88.1.68

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

Mervyn J. Miles^*, Helen J. Carr, Terence C. Mcmaster, Kenneth J. I'Anson, Peter S. Belton, Victor J. Morris, J. Michael Field, Peter R. Shewry, Arthur S. Tatham

^*Corresponding author for this work

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114 Citations (Scopus)

Abstract

Scanning tunneling microscopy has been used to demonstrate that a spiral structure based on β-reverse turns is adopted by the repeat sequences present in a group of wheat gluten proteins. This structure is similar to the β-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.

Original language	English
Pages (from-to)	68-71
Number of pages	4
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	88
Issue number	1
DOIs	https://doi.org/10.1073/pnas.88.1.68
Publication status	Published - 1 Jan 1991
Externally published	Yes

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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. (1991). Scanning tunneling microscopy of a wheat seed storage protein reveals details of an unusual supersecondary structure. Proceedings of the National Academy of Sciences of the United States of America, 88(1), 68-71. https://doi.org/10.1073/pnas.88.1.68

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abstract = "Scanning tunneling microscopy has been used to demonstrate that a spiral structure based on β-reverse turns is adopted by the repeat sequences present in a group of wheat gluten proteins. This structure is similar to the β-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.",

author = "Miles, {Mervyn J.} and Carr, {Helen J.} and Mcmaster, {Terence C.} and I'Anson, {Kenneth J.} and Belton, {Peter S.} and Morris, {Victor J.} and Field, {J. Michael} and Shewry, {Peter R.} and Tatham, {Arthur S.}",

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Miles, MJ, Carr, HJ, Mcmaster, TC, I'Anson, KJ, Belton, PS, Morris, VJ, Field, JM, Shewry, PR & Tatham, AS 1991, 'Scanning tunneling microscopy of a wheat seed storage protein reveals details of an unusual supersecondary structure', Proceedings of the National Academy of Sciences of the United States of America, vol. 88, no. 1, pp. 68-71. https://doi.org/10.1073/pnas.88.1.68

Scanning tunneling microscopy of a wheat seed storage protein reveals details of an unusual supersecondary structure. / Miles, Mervyn J.; Carr, Helen J.; Mcmaster, Terence C. et al.
In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 88, No. 1, 01.01.1991, p. 68-71.

Research output: Contribution to journal › Article › peer-review

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AB - Scanning tunneling microscopy has been used to demonstrate that a spiral structure based on β-reverse turns is adopted by the repeat sequences present in a group of wheat gluten proteins. This structure is similar to the β-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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Scanning tunneling microscopy of a wheat seed storage protein reveals details of an unusual supersecondary structure

Abstract

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