Idpflex: Analysis of Intrinsically Disordered Proteins by Comparing Simulations to Small Angle Scattering Experiments.

It is estimated that about 30% of the eucariotic proteome consists of intrinsically disordered proteins (IDP's), yet their presence in public structural databases is severely underrepresented.IDP's adopt heterogeneous inter-converting conformations with similar probabilities, preventing resolution of structures with X-Ray diffraction techniques.An alternative technique with wide application on IDP systems is small angle scattering (SAS).SAS can measure average structural features of IDP's when in vitro solution, or even at conditions mimicking protein concentrations found in the cell's cytoplasm.