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Table 1 Putative peptide or EGS-crosslinked peptides identified from complete trypsinolysis of EGS-crosslinked HbII.

From: Quaternary structure of Artemia haemoglobin II: analysis of T and C polymer alignment and interpolymer interface

Mass/charge ratio (m/z) Charge statea Putative peptide species
   (Peptide assignment receiving best SearchXlinks score)
   Peptide 1b Polymer, Domainc Peptide 2b Polymer, Domainc SXL Score Noted
626.462f +2 715-FSSIGK-720 TP, Domain 5 883-QLK-885 TP or CP, Domain 6 11.5 XLP
648.457 +2 738-EHIK R-742 TP or CP, Domain 5 883-QLK-885 TP or CP, Domain 6 6.0 XLP
927.400e,f +1 931-GFK-933 TP, Domain 6 931-GFK-933 CP, Domain 6 21.0 XLP
983.462 +1 1138-IFTKVFTK-1145 TP, Domain 8 - - 10.0 UmP
1273.996 +1 68-NIPASELASSER-79 TP, Domain 1 - - 16.0 UmP
1405.492 +1 672-VFAK-675 TP or CP, Domain 5 742-RGLSRK-747 TP or CP, Domain 5 11.5 XLP
1418.573e,f +1 301-ASWNK-305 TP or CP, Domain 2 29-ATIK R-33 TP or CP, Domain 1 130.5 XLP
1542.509f +1 1016-HAISVTTK-1023 TP or CP, Domain 7 493-EAIK-496 CP, Domain 4 153.0 XLP
Mass/charge ratio (m/z) Charge state a Mass/charge Ratio Expected (m/z) Total Possible Peptide Assignment     
626.462f +2 626.323 6     
648.457 +2 648.348 7     
927.400e,f +1 927.446 1     
983.462 +1 983.593 5     
1273.996 +1 1273.639 17     
1405.492 +1 1405.780 20     
1418.573e,f +1 1418.727 5     
1542.509f +1 1541.806 38     
  1. a Charge state of the peaks were inferred from the ESI-MS zoom scan data obtained. The inferred charged states were confirmed by consulting the PMF.
  2. b Crosslinked lysines were in bold.
  3. c TP, T polymer; CP, C polymer.
  4. d XLP, EGS-crosslinked peptides; UmP, unmodified peptide.
  5. e Statistical significances of b and y-type ion matchings were measured for these peaks (See also Table 2).
  6. f Further identifications of peaks remaining unannotated after SearchXlinks scoring were done for these peaks, and afterwards a majority of significant peaks were identified. [See Additional file 1, 2, 3, 4]