Before revision: Many pairwise additive force fields parameterized to reproduce folded protein structures are in active use for intrinsically disordered proteins (IDPs) and regions (IDRs), most of which are found to disagree with solution experiments for the disordered states. Recent modifications of protein-water and water-water energetic interactions in these standard force fields have sought to increase agreement with solution experiments of IDPsand IDRswhile also maintaining the ability to describe folded protein structures. Many-body potentials that include polarization should provide a better physical model for capturing proteins with and without intrinsic disorder, but in this case testing has been more limited for proteins of either class .
After revision: Many pairwise additive force fields parameterized to reproduce folded protein structures are in active use for intrinsically disordered proteins (IDPs) and regions (IDRs), some of which modify energetic terms to improve description of IDPs/IDRs, but are largely in disagreement with solution experiments for the disordered states .