Competition between protein folding and aggregation: A three-dimensional lattice-model simulation

Abstract

A simple lattice model for protein folding was extended to simulate protein association in multichain systems. The model was designed to examine the competition between intramolecular interactions leading to the native protein structure and intermolecular association resulting in the formation of aggregates of misfolded chains. It was found that when three or more molecules interacted, clusters of misfolded chains could be more stable than aggregates of native folds.