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Selective association of protein molecules followed by mass spectrometry

Published online by Cambridge University Press:  01 June 1999

HANS VIS ,
CHRISTOPHER M. DOBSON  and
CAROL V. ROBINSON
HANS VIS
Affiliation:
Oxford Centre for Molecular Sciences, New Chemistry Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QT, United Kingdom
CHRISTOPHER M. DOBSON
Affiliation:
Oxford Centre for Molecular Sciences, New Chemistry Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QT, United Kingdom
CAROL V. ROBINSON
Affiliation:
Oxford Centre for Molecular Sciences, New Chemistry Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QT, United Kingdom
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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.

Keywords

HU proteinsnanoflow electrospray mass spectrometryprotein interactions
Type
ACCELERATED COMMUNICATION
Information
Protein Science , Volume 8 , Issue 6 , June 1999 , pp. 1368 - 1370
Copyright
© 1999 The Protein Society

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