Abstract
Molecules that form structurally specific noncovalent associations in solution are of fundamental biological importance. The weak bonds that constitute these liquid-phase noncovalent complexes determine their strength of interaction, which is indicated by the dissociation constant (K d ). Electrospray ionization mass spectrometry (ESI-MS) is rapidly becoming a useful technique for the detection of specific noncovalent complexes, and potentially for probing relative stabilities for these complexes. Several types of noncovalent association in solution, including enzyme-substrate, receptor-ligand, host-guest, protein-nucleic acid, and oligonucleotide interactions have been demonstrated to survive transfer into the gas phase using ESI (1–4). Through the careful control of instrumental variables in the electrospray atmosphere-vacuum interface region, these complexes can be detected intact.
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References
Smith, R. D., Light-Wahl, K. J., Winger, B. E., and Loo, J. A. (1992) Preservation of non-covalent associations in electrospray ionization mass spectrometry multiply charged polypeptide and protein dimers. Org. Mass Spectrom. 27, 811–821.
Ganem, B. and Henion, J. D. (1993) Detecting noncovalent complexes of biological macromolecules new applications of ion-spray mass spectrometry. Chem. Tracts-Org. Chem. 6, 1–22.
Smith, R. D. and Light-Wahl, K. J. (1993) The observation of non-covalent interactions in solution by electrospray ionization mass spectrometry: promise, pitfalls and prognosis. Biol. Mass Spectrom. 22, 493–501.
Light-Wahl, K. J., Schwartz, B. L., and Smith, R. D. (1994) Observation of the noncovalent quaternary associations of proteins by electrospray ionization mass spectrometry. J. Am. Chem. Soc. 116, 5271–5278.
Winger, B. E., Light-Wahl, K. J., Ogorzalek Loo, R. R., Udseth, H. R., and Smith, R. D. (1993) Observation and implications of high mass-to-charge ratio ions from electrospray ionization mass spectrometry. J. Am. Soc. Mass Spectrom. 4, 536–545.
Gale, D. C., Goodlett, D. R., Light-Wahl, K. J., and Smith, R. D. (1994) Observation of duplex DNA-drug noncovalent complexes by electrospray ionization mass spectrometry. J. Am. Chem. Soc. 116, 6027, 6028.
Bruce, J. E., Van Orden, S. L., Anderson, G. A., Hofstadler, S. A., Sherman, M. G., Rockwood, A. L., and Smith, R. D. (1995) Selected ion accumulation of noncovalent complexes in a Fourier transform ion cyclotron resonance mass spectrometer. J. Mass Spectrom. 30, 124–133.
Gale, D. C. and Smith, R. D. (1993) Small volume and low flow-rate electrospray ionization mass spectrometry of aqueous samples. Rapid Commun. Mass. Spectrom. 7, 1017–1021.
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© 1996 Humana Press Inc., Totowa, NJ
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Schwartz, B.L., Gale, D.C., Smith, R.D. (1996). Noncovalent Interactions Observed Using Electrospray Ionization. In: Chapman, J.R. (eds) Protein and Peptide Analysis by Mass Spectrometry. Methods in Molecular Biology™, vol 61. Humana Press. https://doi.org/10.1385/0-89603-345-7:115
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DOI: https://doi.org/10.1385/0-89603-345-7:115
Publisher Name: Humana Press
Print ISBN: 978-0-89603-345-0
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