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Nanomechanical force measurements of gliadin protein interactions
Author(s) -
Paananen A.,
Tappura K.,
Tatham A. S.,
Fido R.,
Shewry P. R.,
Miles M.,
McMaster T. J.
Publication year - 2006
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.20603
Subject(s) - gliadin , chemistry , globular protein , urea , preprint , polymer science , chemical engineering , biophysics , crystallography , gluten , biochemistry , physics , quantum mechanics , engineering , biology
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 This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com