Proteins which are intrinsically disordered or contain intrinsically disordered regions (IDRs) often play crucial biological roles in protein-protein interactions, however, their disordered nature can make them difficult to study as they may be unstable and prone to aggregation. It has previously been observed in the laboratory that intrinsic dimerisation domains can apparently stabilise IDRs, despite playing no direct role in the interaction. Thus we are trying to engineer protein constructs that incorporate dimerisation domains in order to artificially stabilise IDRs for further study. These designs are initially being tested in yeast two-hybrid assays involving the intrinsically disordered LIM binding domain from DEAF1 binding to LMO4; this interaction can only be detected if a coiled-coil domain from DEAF is also part of the construct. Constructs have been designed to test the ability of N- or C-terminal or both N-and C-dimerisation domains on the IDR from DEAF1 have a stabilising effect. The constructs will also be characterised in terms of expression, stability and biophysical properties in bacterial and mammalian systems, and applied to other IDRs that are implicated in binding events that have been difficult to validate by standard assays used for globular proteins.