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Nanoflow electrospray mass spectrometry was used to monitor the formation of protein heterodimers of HU proteins from Bacillus stearothermophilus and Bacillus subtilis. This has enabled us to analyze both thermodynamic and kinetic features associated with the dissociation of homodimeric HU proteins. The results obtained correlate well with the kinetics of the protein dissociation process and the free energy difference between homo- and heterodimeric species anticipated from other studies. We suggest that this approach will have general applicability in studying protein association and dissociation under near-equilibrium conditions and will be relevant to a wide range of biological systems.

Original publication




Journal article


Protein Sci

Publication Date





1368 - 1370


Bacillus subtilis, Bacterial Proteins, DNA-Binding Proteins, Dimerization, Geobacillus stearothermophilus, Kinetics, Mass Spectrometry, Thermodynamics