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. 2009 Jun;18(6):1272–1280. doi: 10.1002/pro.139

Figure 2.

Figure 2

High resolution ESI/FTMS analysis of AgCARM1WT expressed in E. coli. Top, ESI/FTMS spectrum of AgCARM1WT intact protein ions (M44+), suggesting AgCARM1WT is predominantly dimethylated. Bottom, fragmentation map from 3 ECD and 6 CAD spectra of both un- and di-methylated AgCARM1WT matched with assignments to the DNA-predicted sequence of AgCARM1WT with the removal of N-terminal methionine, localizing the dimethylation site to R485 (highlighted in circle). The fragmentation ions containing the dimethylated form were indicated in dots.