Nanomechanical force measurements of gliadin protein interactions

A Paananen, K Tappura, AS Tatham, R Fido, PR Shewry, MJ Miles, TJ McMaster

Research output: Contribution to journalArticle (Academic Journal)peer-review

12 Citations (Scopus)

Abstract

The strength and nature of interactions between monomeric gliadin proteins involving alpha-alpha, omega-omega, and alpha-omega interactions in 0.01M acetic acid, and the effect of urea has been investigated. It was shown by means of nanomechanical force measurements that the stretching events in the separation curve after adhesive phenomena originated from proteins. These stretching events displayed different responses of the alpha- and omega-gliadins to area. While 2M urea caused the more globular alpha-gliadins to unfold, the beta-turn-rich omega-gliadins remained fairly stable even in 8M urea. This suggests different roles for gliadins in the formation of dough; while the omega-gliadins are still in a compact structure being responsible for the viscous,flow, the a-gliadins have already started to participate informing the network in dough.
Translated title of the contributionNanomechanical force measurements of gliadin protein interactions
Original languageEnglish
Pages (from-to)658 - 667
Number of pages10
JournalBiopolymers
Volume83(6)
DOIs
Publication statusPublished - Dec 2006

Bibliographical note

Publisher: John Wiley and Sons Inc

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