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. Author manuscript; available in PMC: 2013 Feb 15.
Published in final edited form as: Anal Biochem. 2011 Dec 13;421(2):712–718. doi: 10.1016/j.ab.2011.12.012

Figure 3. Internal cross-linking distant lysine residues using non-cleavable linker.

Figure 3

Panel a: The MS/MS analysis of the precursor ion with 1959.89 m/z (~86kDa in Fig. 1 a) linked with 11.4Å linker presents fragment ion assignment for peptide H2N-DSQEEEKTEALTSAKR-COOH with the cross-linker molecule linking both lysine residues present in this peptide. The ions containing the mass of the arm were labeled with subscript (arm). Panel b shows that the linked lysine side chains are in opposite directions and the distance between the ε-amines of both lysine residues is 20.4Å.