Multimeric self-assembly equilibria involving the histone-like protein H-NS - A thermodynamic study

The thermodynamic parameters affecting protein-protein multimeric self-asse mbly equilibria of the histone-like protein H-NS were quantified by "large zone" gel-permeation chromatography. The abundance of the different associa tion states (monomer, dimer, and tetramer) were found to be strictly depend ent on the monomeric concentration and affected by physical (temperature) a nd chemical (cations) parameters. On the basis of the results obtained in t his study and the available structural information concerning this protein, a mechanism is proposed to explain the association behavior also in relati on to the functional properties of the protein.