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The extent of coupling between the folding of a protein and its binding to asubstrate varies from protein to protein. Some proteins have highly structurednative states in solution, while others are natively disordered and only foldfully upon binding. In this Letter, we use Monte Carlo simulations toinvestigate how disordered polymer chains grafted around a binding site affectthe folding and binding of three model proteins. The protein that approachesthe substrate fully folded is more hindered during the binding process thanthose whose folding and binding are cooperative. The polymer chains act aslocalized crowding agents and can select correctly folded and boundconfigurations in favor of non-specifically adsorbed states. The free energychange for forming all intra-protein and protein-substrate contacts can dependnon-monotonically on the polymer length.

Controlling the folding and substrate-binding of proteins using polymer brushes