Electrospray ionization has made possible the transference of non-covalently bound complexes from solution phase to high vacuum. In the process, a complex acquires a net charge and becomes amenable to measurement by MS. FTICR (Fourier-transform ion cyclotron resonance) MS allows these ions to be measured with sufficiently high resolution for the isotopomers of complexes of small proteins to be resolved from each other (true for complexes up to about 100 kDa for the most powerful FTICR instruments), which is of crucial significance in the interpretation of spectra. Results are presented for members of the S100 family of proteins, demonstrating how non-covalently bound complexes can be distinguished unambiguously from covalently bound species. Consideration relevant both to determination of binding constants in solution from the gas-phase results and to the elucidation of protein folding and unfolding in solution are discussed. The caveats inherent to the basic approach of using electrospray and MS to characterize protein complexes are weighed and evaluated.
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October 2003
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Conference Article|
October 01 2003
Protein–ligand and protein–protein interactions studied by electrospray ionization and mass spectrometry
W.I. Burkitt;
W.I. Burkitt
*Department of Chemistry, University of Warwick, Coventry CV4 7AL, U.K.
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P.J. Derrick;
P.J. Derrick
1
*Department of Chemistry, University of Warwick, Coventry CV4 7AL, U.K.
1To whom correspondence should be addressed (e-mail p.j.derrick@warwick.ac.uk).
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D. Lafitte;
D. Lafitte
†Faculte de Pharmacie, 27 Boulevard Jean Moulin, 13385 Marseille Cedis 05, France
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I. Bronstein
I. Bronstein
‡Institute of Animal Health, Protein Structure Group, Compton Laboratory, Compton, Newbury RG20 7NN, U.K.
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Publisher: Portland Press Ltd
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2003 Biochemical Society
2003
Biochem Soc Trans (2003) 31 (5): 985–989.
Citation
W.I. Burkitt, P.J. Derrick, D. Lafitte, I. Bronstein; Protein–ligand and protein–protein interactions studied by electrospray ionization and mass spectrometry. Biochem Soc Trans 1 October 2003; 31 (5): 985–989. doi: https://doi.org/10.1042/bst0310985
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