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. Author manuscript; available in PMC: 2013 Jun 4.
Published in final edited form as: Angew Chem Int Ed Engl. 2012 Apr 23;51(23):5692–5695. doi: 10.1002/anie.201109127

Figure 2.

Figure 2

(A) Plot of the measured average mass increase relative to the sequence mass of TTR as a function of trap collision voltage for a range of cation additives. The approximate numbers of cations that stay strongly bound to the protein assembly even at large trap collision voltage are shown on the right. (B) A plot of the average CID versus CIU collision energies (eV*) for the 5 protein complexes studied for each cation additive. The protein-cation complexes have highly-correlated unfolding and dissociation energies (dashed line). (C) Data from Fig. 2B plotted against the charge-per-unit-area of the cations added (vertical axis) illustrate a well-correlated relationship between protein-cation complex stability and the charged area of added cations.