抄録
Coupled folding and binding exhibited by intrinsically disordered proteins (IDPs) was reproduced computationally by an enhanced conformational sampling method, multicanonical molecular dynamics. We treat biomolecules with an all-atom model immersed in an explicit solvent. A free-energy landscape, which is a road map for the biomolecular conformational changes, has been computed for two IDP-partner systems (NRSF–mSin3 and pKID–KIX). Native and non-native complex clusters distributed in the landscape, and free-energy barriers separated those clusters. Analyses have suggested that various encounter complexes can reach the native complex via multiple pathways with overcoming the free-energy barriers.
