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Selective association of protein molecules followed by mass spectrometry
Author(s) -
Vis Hans,
Dobson Christopher M.,
Robinson Carol V.
Publication year - 1999
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.8.6.1368
Subject(s) - bacillus subtilis , mass spectrometry , dissociation (chemistry) , chemistry , kinetics , electrospray , molecule , biophysics , chromatography , biology , bacteria , organic chemistry , genetics , physics , quantum mechanics
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.