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In the grain, wheat storage proteins form assemblies in the grain called protein bodies. These assemblies are formed by interactions that depend on  biological microenvironment but also on intrinsic structural characteristics of the proteins, whose structures have not been resolved yet.

In an effort to probe these characteristics, we set out to study a wheat protein, y-gliadin, and each of its N-terminal (N-ter) and C-terminal (C-ter) domains obtained after partial hydrolysis.

These proteins are known to show broad structural and conformational flexibility, yet the roles played by N-ter and C-ter are unclear.

Biochemical and structural methods (dichroism spectra, small-angle X-ray scattering, ab initio computational modelling) were developed to determine whether or not y-gliadin is intrinsically disordered.

Based on our evidence, we learned that the wheat y-gliadin is partially disordered, with a disordered N-ter domain and an ordered C-ter domain. We went on to propose a new three-dimensional model of y-gliadin on the basis of ab initio computations and small-angle X-ray scattering curves.