Table 1 of
Peterson, Mol Vis 2004;
10:857-866.Table 1 of
Peterson, Mol Vis 2004;
10:857-866.
Table 1. Sequences assigned to experimental m/z for tryptic peptides
Summary of sequences assigned to experimental mass to charge ratios (m/z) for tryptic peptides based on sequencing data or mass correlation. Experimental masses from different cross-linking reactions were compared across each row to search for structures that were equivalent apart from the structure of the cross-linker. Rows with more than one experimental mass have structures from different cross-linking experiments that are correlated. Note three different changes in mass (Δm=+12, +24, or +42) were considered as a result of cross-linking and/or modification by formaldehyde [32]. If no correlated ion was found within 200 ppm of the theoretical m/z for the modification, the designation "NO" (Not observed) was entered. Measured m/z for product ions resulting from the different reagent treatments are shown in black font. Theoretical m/z of these ions are shown in red. Ion charges greater than one are reported in parenthesis. Numbered lysines denote confirmed or possible sites of modification by formaldehyde (FA) or DTSSP. The sharp (hash mark) indicates that the singly deamidated species was also observed at a different retention time and sequenced. Its mass is not listed. The single asterisk indicates that these ions have been sequenced using collision induced decay (CID). The double asterisk indicates that no correlation was observed, but loss of Ac-Met and extensive loss of Arg was observed. The triple asterisk indicates that the deamidated species was observed. The "at" symbol (@) indicates oxidation of methionine was observed. Conclusions derived from each deduced product are listed in the final column.
FA
-----------------------------------
Name Sequence DTSSP Δm=+12.00 Δm=+24.00 Δm=+42.01 Conclusion
---------- -------------------------------- ----------- ----------- --------- --------- -------------------
αA1-12*# Ac-MDIAIQHPWFK11R 1775.8 1596.1 NO NO K11 of αA solvent
1775.82 1595.82 accessible
αA71-88* FVIFLDVK78HFSPEDLTVK 2326.2 NO NO NO K78 of αA solvent
2326.17 accessible
αA89-103*# VQEDFVEIHGK99HNER 2027.9 NO NO NO K99 of αA solvent
2027.9 accessible
αB164-175 EEK166PAVTAAPK174K 1460.9 NO NO 1310.9 K166 or K174 of αB
1460.73 1310.73 solvent accessible
α164-175 EEK166PAVTAAPK174K 1442.9 NO NO 1310.9 K166 and K174 of αB
(Intrapeptide crosslink) 1442.72 1310.73 solvent accessible
αB70-74 LEK72DR-APSWIDTGLSEMRLEK72DR 1469.0 (2) 1396.0 (2)@ NO NO K72 of αB involved
αB57-74 1469.21 (2) 1396.21 (2) in αB-αB subunit
interaction
αB70-74 LEK72DR-LEK72DRFSVNLDVK 1198.8 (2) 2235.2*** NO NO K72 of αB involved
αB70-82 1198.61 (2) 2234.21 in αB-αB subunit
interaction
αB150-157 K150QASGPER-TIPITREEK166PAVTAAPK 1434.5 (2) 1353.4 (2) NO NO K150 and K166 of αB
αB158-174 1434.25 (2) 1353.25 (2) involved in
intramolecular
crosslinking or
αB-αB subunit
interactions
αB117-123 EFHRK121YR-VQEDFVEIHGK99HNER 1523.6 (2) 1442.0 (2) NO NO K121 of αB and K99
αA89-103 1523.22 (2) 1442.22 (2) of αA involved in
αB-αA interactions
αB117-123 EFHRK121YR-Ac-MDIAIEHPWFK11R NO NO 2643.17** NO K121 of αB and K11
αA1-12** 2642.35 of αA involved in
αB-αA interactions
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