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. Author manuscript; available in PMC: 2009 Apr 1.
Published in final edited form as: J Proteome Res. 2008 Aug 14;7(10):4225–4236. doi: 10.1021/pr800044q

Figure 3.

Figure 3

A. Broadband mass spectrum of the 8+, 9+ and 10+ charge states of the histone H3.2(1-50) polypeptide from rat kidney. Further isolation of the 8+ charge state species is achieved through additional quadrupole enhancement and SWIFT isolation as shown in the inset mass spectrum. B. ECD fragmentation of the 8+ charge state species isolated in (A.). Zoom regions spanning 528-552 m/z and 895-912 m/z show regions containing fragment ions which correspond to posttranslational modifications on K9 (unmodified, mono-, di- and trimethylation) and K36 (unmodified, mono- and dimethylation), respectively. C. ECD fragment map generated from the fragmentation spectrum shown in (B.). Some of the most common modifications observed on histone H3.2 from rat kidney are K9me2K23acK27me2K36me2.