On the elasticity of wheat gluten
1999
Belton, P.S.
The nature of the interprotein interactions in wheat gluten is discussed with particular reference to the role of the high molecular weight subunits. It is argued that the high molecular weight subunits interact with each other by disulphide bonds and hydrogen bonds. Dough working favours the formation of end to end disulphide bonds in the subunits and this increases the effective molecular weight of the subunit and hence the number of protein-protein interactions. Association of the subunits can also take place by interchain hydrogen bonding. So many hydrogen bonds are formed that not all can be broken simultaneously although there will be unbonded mobile regions (loops) and bonded regions (trains). Stretching extends loops and then causes the proteins to slide over one another. The elastic restoring force is provided by the re-establishment of the loop train equilibrium.
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