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. Author manuscript; available in PMC: 2018 Feb 1.
Published in final edited form as: J Am Soc Mass Spectrom. 2016 Oct 12;28(2):332–340. doi: 10.1007/s13361-016-1517-7

Figure 5.

Figure 5

(a) The percent Zmax (circle) and Zav (square) of ZR, for protein ions formed from aqueous ammonium acetate (filled markers) or pure water (open markers) prior to reaction with a base v. the decrease in Zmax (circle) and Zav (square) after 120 s reaction with DPA. (b) fraction of basic residues, (c) molecular weight (d) number of basic residues (e) isoelectric point (pI) for each protein as a function of the decrease in Zmax (circle) and Zav (square) after 120 s reaction with DPA. (i) corresponds to cytochrome c, (ii) myoglobin, (iii) carbonic anhydrase, (iv) concanavalin A dimer and (v) holo-transferrin ions, respectively.