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. Author manuscript; available in PMC: 2011 Jan 15.
Published in final edited form as: Anal Chem. 2010 Jan 15;82(2):579–584. doi: 10.1021/ac9018582

Table 4.

Frequency of matching different ion types in ETD spectra of peptides produced by different cleavages. Numbers represent the fraction of all matched peaks in a given spectrum that match to each ion type. Results are separated into those from doubly-charged precursor ions and those of a higher charge state. (Note: tryptic numbers differ slightly from Table 3 due to the lack of consideration of ‘x’ ions).

Enzyme Prec. Charge LysC 2+ LysC >2+ LysN 2+ LysN >2+ CNBr 2+ CNBr >2+ Trypsin 2+ Trypsin >2+
b 0.02 0.03 0.06 0.04 0.04 0.05 0.03 0.03
c-1 0.11 0.05 0.17 0.06 0.14 0.08 0.10 0.04
c 0.20 0.33 0.49 0.42 0.31 0.36 0.11 0.34
y 0.13 0.09 0.05 0.06 0.06 0.06 0.14 0.11
z 0.30 0.29 0.17 0.27 0.27 0.25 0.31 0.31
z+1 0.23 0.20 0.07 0.15 0.18 0.21 0.32 0.17