Detection of multiple protein conformational ensembles in solution via deconvolution of charge-state distributions in ESI MS.
Monitoring the changes in charge-state distributions of protein ions in electrospray ionization (ESI) mass spectra has become one of the commonly accepted tools to detect large-scale conformational changes of proteins in solution. However, these experiments produce only qualitative, low-resolution information. Our goal is to develop a procedure that would produce quantitative data on protein conformational isomers coexisting in solution at equilibrium. To that end, we have examined the evolution of positive ion charge-state distributions in the
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Department of Chemistry, University of Massachusetts, Amherst 01003, USA.
Kaltashov
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D000818:Animals; D004563:Electrochemistry; D006736:Horses; D006863:Hydrogen-Ion Concentration; D009211:Myoglobin / Q000737:chemistry*; D011487:Protein Conformation; D017510:Protein Folding; D018168:Receptors, Retinoic Acid / Q000737:chemistry*; D021241:Spectrometry, Mass, Electrospray Ionization / Q000379:methods*
D009211:Myoglobin; D018168:Receptors, Retinoic Acid; C082927:retinoic acid binding protein I, cellular