Title |
Increasing charge while preserving noncovalent protein complexes for ESI-MS
|
---|---|
Published in |
Journal of the American Society for Mass Spectrometry, November 2008
|
DOI | 10.1016/j.jasms.2008.11.013 |
Pubmed ID | |
Authors |
Shirley H. Lomeli, Sheng Yin, Rachel R. Ogorzalek Loo, Joseph A. Loo |
Abstract |
Increased multiple charging of native proteins and noncovalent protein complexes is observed in electrospray ionization (ESI) mass spectra obtained from nondenaturing protein solutions containing up to 1% (vol/vol) m-nitrobenzyl alcohol (m-NBA). The increases in charge ranged from 8% for the 690 kDa alpha(7)beta(7)beta(7)alpha(7) 20S proteasome complex to 48% additional charge for the zinc-bound 29 kDa carbonic anhydrase-II protein. No dissociation of the noncovalently bound ligands/subunits was observed upon the addition of m-NBA. It is not clear if the enhanced charging is related to altered surface tension as proposed in the "supercharging" model of Iavarone and Williams (Iavarone, A. T.; Williams, E. R. J. Am. Chem. Soc.2003, 125, 2319-2327). However, more highly charged noncovalent protein complexes have utility in relaxing slightly the mass-to-charge (m/z) requirements of the mass spectrometer for detection and will be effective for enhancing the efficiency for tandem mass spectrometry studies of protein complexes. |
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