Increasing Charge While Preserving Noncovalent Protein Complexes for ESI-MS
In: Journal of the American Society for Mass Spectrometry, Jg. 20 (2009), Heft 4, S. 593-596
Online
academicJournal
- print, 27 ref
Zugriff:
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 α7β7β7α7 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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Increasing Charge While Preserving Noncovalent Protein Complexes for ESI-MS
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Autor/in / Beteiligte Person: | LOMELI, Shirley H ; SHENG, YIN ; OGORZALEK LOO, Rachel R ; LOO, Joseph A |
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Zeitschrift: | Journal of the American Society for Mass Spectrometry, Jg. 20 (2009), Heft 4, S. 593-596 |
Veröffentlichung: | Amsterdam: Elsevier, 2009 |
Medientyp: | academicJournal |
Umfang: | print, 27 ref |
ISSN: | 1044-0305 (print) |
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