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. 2009 Oct 27;284(52):36128–36136. doi: 10.1074/jbc.M109.043448

FIGURE 6.

FIGURE 6.

Summary of all detected GlyRα1 ECD peptides and their modifications. The complete amino acid sequence of the bacterial expression construct is shown. Bars indicate observed tryptic fragments as detected by MALDI-TOF mass spectrometry. Theoretical monoisotopic molecular masses (Da) are given for each fragment. Where essential, corresponding average molecular masses are given in brackets. Redundant fragments resulting from limited proteolysis are omitted. The number of asterisks (*) indicates the number of observed lysine modifications for each peptide. Cysteine residues are confirmed by mass shifts of the respective fragments upon N-maleoyl-β-alanine (N-M-β-A) modification and serine substitution (#). Brackets connect cysteine residues that are found to form disulfide bonds. The total sequence coverage is greater than 95%.