Divide and conquer: partial hydrolysis of a wheat protein

The reserve proteins of wheat form in the grain assemblies, called protein corpuscles. These assemblies are formed by interactions which depend on the biological medium but also on the intrinsic structural characteristics of the proteins. However, their structure has not been resolved to date.

In order to probe these characteristics, we undertook a study of a wheat protein, y-gliadin, and its two N-terminal (N-ter) and C-terminal (C-ter) domains obtained after partial hydrolysis.

The results made it possible to demonstrate the partially disordered nature of the y-gliadin, with a disordered N-ter domain and an ordered C-ter domain. A new three-dimensional model of y-gliadin could be proposed based on ab initio modeling and small-angle X-ray scattering.