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GrainGenes Reference Report: BBA-1548-187

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Reference	BBA-1548-187
Title	Wheat seed proteins exhibit a complex mechanism of protein elasticity
Journal	Biochimica et Biophysica Acta-Protein Structure and Molecular Enzymology
Year	2001
Volume	1548
Pages	187-193
Author	Tatham AS Hayes L Shewry PR Urry DW
Abstract	Summary: Elastomeric proteins are found in a number of animal tissues (elastin, abductin and resilin), where they have evolved to fulfil a range of biological functions. All exhibit rubber-like elasticity, undergoing deformation without rupture, storing the energy involved in deformation, and then recovering to their initial state when the stress is removed. The second part of the process is passive, entropy decreasing when the proteins are deformed, with the higher entropy of the relaxed state providing the driving force for recoil. In plants there is only one well-documented elastomeric protein system, the alcohol-soluble seed storage proteins (gluten) of wheat. The elastic properties of these proteins have no known biological role, the proteins acting as a store for the germinating seed. Here we show that the modulus of elasticity of a group of wheat gluten subunits, when cross-linked by gamma-radiation, is similar to that of the cross-linked polypentapeptide of elastin. However, thermoelasticity studies indicate that the mechanism of elastic recoil is different from elastin and other characterized protein elastomers. Elastomeric force, f, has two components, an internal energy component, f(e), and an entropic component, f(s). The ratio f(e)/f can be determined experimentally; if this ratio is less than 0.5 the elastomeric force is predominantly entropic in origin. The ratio was determined as 5.6 for the cross-linked high M(r) subunits of wheat glutenin and near zero for the cross-linked polypentapeptide of elastin. Tensile stress must be entropic or energetic in origin, the results would suggest that elastic recoil in the wheat gluten subunits, in part, may be associated with extensive hydrogen bonding within and between subunits and that entropic and energetic mechanisms contribute to the observed elasticity. Total number of records in report: 22
Keyword	[ Hide all but 1 of 41 ] biochemistry biological function biophysics complexes component deformation elasticity energy force function gamma gamma radiation gluten glutenin high m r subunits hydrogen m-r m-r subunits mechanism modulus of elasticity origin peptide properties protein radiation seed seed protein seed storage seed storage protein sequence spider silk state storage storage protein stress subunit system tissue wheat gluten wheat glutenin wheat seed

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