Investigating families of intrinsically disordered proteins that fold upon binding. 
 One particularly useful approach for investigating protein folding is 'to investigate the folding of several topologically, structurally and/or evolutionarily related proteins in order to discern patterns and trends in folding (stability, pathways and mechanisms). We are now applying this approach to the folding of intrinsically disordered proteins.
 The systems we are studying all involve formation of helical structure when a disordered protein binds its target. The properties of these systems are vastly different, binding affinity ranges from µM – nM and association and disassociation rate constants vary by many orders of magnitude. This brings different challenges for determining the kinetics of assembly and disassembly.
 We are investigating some fundamental questions in the IDP field: How important is residual structure in the IDP‾ How do regions outside the binding site influence binding‾ What are the mechanisms of binding‾ What role does the partner protein play in determining the binding mechanism and the strength of binding‾ Can we relate biophysical properties to specific IDP functions‾
 I will discuss our latest findings.