Nanomechanical force measurements of gliadin protein interactions

A - Papers appearing in refereed journals

Paananen, A., Tappura, K., Tatham, A. S., Fido, R., Shewry, P. R., Miles, M. and Mcmaster, T. J. 2006. Nanomechanical force measurements of gliadin protein interactions. Biopolymers. 83 (6), pp. 658-667.

AuthorsPaananen, A., Tappura, K., Tatham, A. S., Fido, R., Shewry, P. R., Miles, M. and Mcmaster, T. J.
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. (c) 2006 Wiley Periodicals, Inc.

KeywordsBiochemistry & Molecular Biology; Biophysics
Year of Publication2006
JournalBiopolymers
Journal citation83 (6), pp. 658-667
Digital Object Identifier (DOI)doi:10.1002/bip.20603
PubMed ID16977631
Open accessPublished as non-open access
Funder project or code501
FunderBiotechnology and Biological Sciences Research Council
ISSN00063525
PublisherWiley
Grant IDBBS/E/C/00004226

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