  A significant part of the proteome is composed of intrinsically-disordered
proteins (IDPs). These proteins do not fold into a well-defined structure and
behave like ordinary polymers. In this work we consider IDPs which have the
tendency to aggregate, model them as heteropolymers that contain a small number
of associating monomers and use computer simulations in order to compare the
aggregation of such IDPs that are grafted to a surface or free in solution. We
then discuss how such grafting may affect the analysis of in-vitro experiments
and could also be used to suppress harmful aggregation.
