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Table 1 DeCyder MS analysis for Q-TOF MS of recombinant parkin exposed to H2O2

From: Oxidation of the cysteine-rich regions of parkin perturbs its E3 ligase activity and contributes to protein aggregation

Domain (Residue #) Peptide Sequence Monoiostopioc M r Calculated Observed Modifications Ratio
RING I 235NITCITCTDVR245 1326.59 1326.56 Cys-CAM (C); Cys-SO2H (C) 13.2
(238 - 293) 235NITCITCTDVR245 1333.55 1333.62 2 Cys-SO3H n/a
  235NITCITCTDVRSPVLVFQCNSR256 2605.19 2605.18† Cys-CAM; Cys-SO2H; Cys-SO3H n/a
  246SPVLVFQCNSR256 1296.61 1296.58 Cys-SO3H n/a
  257HVICLDCFHLYCVTRLNDR275 2367.09 2367.19* Cys-SO3H 3.6
IBR 350VTCEGGNGLGCGFAFCRECK369 2154.86 2154.90 Cys-CAM; Cys-SO3H n/a
(294 - 417) 370EAYHEGECSAVFEASGTTTQAYR392 2554.06 2554.09 Cys-SO3H n/a
RING II 428NGGCMHMK435 956.31 956.33 2 Oxidation (Met); Cys-SO3H n/a
(418 - 449) 428NGGCMHMKCPQPQCR442 1882.70 1882.77 2 Cys-CAM; 2 Oxidation (Met); Cys-SO3H n/a
  436CPQPQCR442 862.34 862.40 Cys-SO2H n/a
Others 130DSPPAGSPAGRSIYNSFYVYCK151 2410.09 2410.15 Cys-SO2H (C) 8.1
(1 - 237) 171QATLTLTQGPSCWDDVLIPNR191 2375.14 2375.15 Cys-SO3H (C) n/a
  192MSGECQSPHCPGTSAEFFFK211 2236.89 2236.94 Cys-SO3H (C) 69.1
  192MSGECQSPHCPGTSAEFFFK211 2309.90 2309.93 Cys-CAM (C); Oxidation (Met); Cys-SO3H (C) n/a
  1. Notes: GST-parkin was exposed to 10 μM (unmarked), 50 μM (*), or 200 μM H2O2 (†). To compensate for intensity differences between elution profiles of individual experiments, normalization was performed using the measured intensity distribution of the entire peptide population. Our development of this algorithm represents a novel function of DeCyder MS v2.0. The ratio of peptide modification was calculated as the intensity of H2O2-exposed parkin compared to vehicle-treated control. Peptide sequences in these experiments are determined by mass fingerprint. Legend: n/a, not applicable (since peptide modifications were only identified for the H2O2-exposed samples); IBR, in-between RING domain; CAM, Carbamidomethyl; Cys, cysteine; Met, methionine.