Population balance modeling of assembly formation; accounting for the H-NS protein oligomerization and DNA binding mechanisms

Abstract

The results obtained in this study demonstrate H-NS oligomerization in solution is not sufficient in forming large structures of H-NS-DNA assemblies indicating oligomerization along bacterial DNA is crucial. We present a comprehensive and novel multi-scale modeling scheme to study protein-protein and protein-DNA interactions, with the focus on population balance modeling of assemblies formed by the H-NS protein and bacterial DNA. The model helps understanding how the concentration of H-NS influences the formation of H-NS-DNA assemblies. The presented model covers the two underlying molecular mechanisms involved in assembly formation, H-NS oligomerization in solution and H-NS-DNA binding. Within protein oligomerization interactions, protein molecules are entitled to dimerize, propagate, recombine and deform (break). In addition, DNA binding and unbinding interactions are included to account for formation of filaments along DNA. All mechanisms have been modeled with their associated forward (formation) and backward (deformation) interactions. The results obtained agree well with former experimental studies.