SAXS On IDPs Server

Intrinsically disordered protein (IDP) regions and the denatured state ensemble (DSE) of foldable proteins, lack a single nearly-fixed 3D structure which intern makes studying them difficult. To understand their conformations, small angle X-ray scattering (SAXS) is widely utilized to extract information about the size (quantified as the R_g) and shape (quantified as 𝜈, the solvent quality or preference for protein-protein over protein-solvent interactions). In my graduate work in Tobin Sosnick's lab, I utilized simulations of IDPs to develop an empirical and universal function (called an MFF) to fit SAXS data on homopolymers and reasonably well-mixed heteropolymers typical of IDPs and foldable sequences (Riback et al., (2017) Science , Riback et al (2019) PNAS). To make this tool widely assessable, I developed and periodically update a website for its application to SAXS data on proteins and other polymers. (Link)