Effect of Disruption of the Interface between Monomers in a Dimer on the Structural and Dynamic Properties of the HU Protein from Spiroplasma Melliferum

The effect of replacements of amino-acid residues that form the interface between monomers in a dimer of the HU protein from Spiroplasma Melliferum (HUSpm) on the stability and conformational dynamics of the molecule is investigated. The behavior of single and multiple HUSpm mutants is studied by molecular dynamics. Simulation is carried out using the GROMACS software package, and OPLS is used as a force field. For each mutant, a full-atom simulation is performed with a duration of 50 ns. The data obtained show that disruption of the interface between monomers in the alpha-helical domain increase the mobility of the molecule in the DNA-binding domain.