Abstract
The strength and nature of interactions between monomeric gliadin proteins involving α–α, ω–ω, and α–ω interactions in 0.01__M__ 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 α‐ and ω‐gliadins to urea. While 2__M__ urea caused the more globular α‐gliadins to unfold, the β‐turn‐rich ω‐gliadins remained fairly stable even in 8__M__ urea. This suggests different roles for gliadins in the formation of dough; while the ω‐gliadins are still in a compact structure being responsible for the viscous flow, the α‐gliadins have already started to participate in forming the network in dough.© 2006 Wiley Periodicals, Inc. Biopolymers 83: 658–667, 2006
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