title: Selective association of protein molecules followed by mass spectrometry.
abstract: 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.
authors.affiliation: Oxford Centre for Molecular Sciences, New Chemistry Laboratory, University of Oxford, United Kingdom.
authors.forename: H
authors.initials: H
authors.lastname: Vis
authors.forename: C M
authors.initials: CM
authors.lastname: Dobson
authors.forename: C V
authors.initials: CV
authors.lastname: Robinson
mesh_terms: D001412:Bacillus subtilis / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry*; D004268:DNA-Binding Proteins / Q000737:chemistry*; D019281:Dimerization; D001411:Geobacillus stearothermophilus / Q000737:chemistry*; D007700:Kinetics; D013058:Mass Spectrometry; D013816:Thermodynamics
chemical_list: D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; C040330:histone-like protein HU, bacteria