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Influence of Native-Like and Non-Native Solvent Conditions
Early ESI studies of proteins by Chait and others demonstrated that the charge state distributions were dramatically influenced by solvent conditions. We used the protein ubiquitin as a model system to follow the conformational changes upon ESI from mostly aqueous (90%) and mostly denaturing (90% acetonitrile) solutions.
Relevant
Publications:
Li, J.; Taraszka, J. A.; Counterman, A. E.;
Clemmer, D. E. Influence
of solvent composition and capillary temperature on the conformations of
electrosprayed ions: unfolding of compact ubiquitin conformers from
pseudonative and denatured solutions, Int. J. Mass. Spectrom.
1999, 185/186/187, 37-47.
Last modified: October 23, 2006