Table I All peptides interfering with more than two transitions of AIAGHLVEFFR

Listed are the 13 peptides that share three or more transitions with the target peptide (320 peptides sharing less than three transitions are not shown here). Target transitions are ordered by signal intensity, and signal interference is indicated by ×. For each peptide, the distance to the target peptide in retention time (predicted by SSRCalc) and Q1 is given as well as the number of observations in PeptideAtlas (PA). Although many possible unique ion signatures exist, the experimentally relevant ones are those that contain the most abundant transition signals (indicated by transition rank). The results are valid for SRM settings of 1.2 Th on Q1 and 2.0 Th on Q3; the last four peptides interfere with a higher isotope with the target peptide. Charge states of all precursors are 3+. Transitions are in their order of signal strength: y5+, y6+, y3+, y4+, y7++, y9++, b5+, y7+, y8+, and y8++.

Transition rank12345678910ΔSSRCalcΔQ1PA
SSSVISTPVASPK×××13.070.000
RPSENPFFHK×××12.430.350
ALHFEYPPGTK×××11.780.020
GEAELTFIPQR×××5.320.320
KPSSYVMVPRP×××13.690.330
GQQSITNEDLR×××16.730.310
SILNMLSVIDR×××9.080.348
SPQQQQGHPPR××××29.120.020
LLQLNNDDTSK××××15.950.321
APSDTTFDLYK×××9.590.317
YSTAHLNKPPK×××22.260.332
LPWYVLSSYK×××1.180.340
AIYTSLLHLAR×××0.60.324