Effect of protein stabilization on charge state distribution in positive- and negative-ion electrospray ionization mass spectra
Changes in protein conformation are thought to alter charge state distributions observed in electrospray ionization mass spectra (ESI-MS) of proteins. In most cases, this has been demonstrated by unfolding proteins through acidification of the solution. This methodology changes the properties of the solvent so that changes in the ESI-MS charge envelopes from conformational changes are difficult to separate from the effects of changing solvent on the ionization process. A novel strategy is...[Show more]
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|Source:||Journal of the American Society for Mass Spectrometry|
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