Characterization of RolA aggregation drivers

Some proteins self-assemble to form fibrous structures to express their functions. Considering the natural state in which proteins function, proteins are surrounded by various interfaces, and it is known that interfaces affect self-assembling, but molecular mechanisms of this phenomena is largely unknown. RolA is a globular protein produced by filamentous fungus Aspergillus oryzae. RolA needs to self-assemble in amyloid-like assemblies in order to perform its function. How this self-assembly is tailored by the host is not clear and it seems that contact with different interfaces is critical. In this study, we will analyze the structural and suprastructural states of the proteins in solution, by SAXS, and at the interface using GI-SAXS. The goal is to understand how the protein interacts with various interfaces in order to modulates its self-assembly. Our findings will provide a clear explanation for the ubiquitous, naturally occurring surface-induced protein assembly.