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. Author manuscript; available in PMC: 2011 Jun 1.
Published in final edited form as: Amino Acids. 2010 Mar 22;41(1):7–27. doi: 10.1007/s00726-010-0552-0

Table 4.

Covalently modified tryptic peptides

Sequencea MH+ Charge XCorr
122FF K~ FSRDVFLP K~ PSWGNHTIPF 148R 3017.23 3 2.47
242H FIEQGINV C@ LCQSYA K^ N M* GLYGE 266R 3077.29 3 2.95
267VGAFTVV C@ KDAEEAK 282R 1808.91 3 3.12
55K AEAQIAGKNLD K~ EYLPIGGLADF C# 81K 2945.47 3 4.03
64NLD K~ EYLPIGGLADF C# 81K 2048.96 2 2.41
288K~ ILIRPLYSNNPLNGA 304R 2730.51 3 2.53
283VESQL K~ ILIRPLYSNNPLNGA 304R 2574.40 3 3.13
160YYDP K~ T C# GFDFSGALEDIS 179K 2409.02 2 2.79
3ASSWWTHVEMGPPDPILGVTEAF 25K~ 2907.30 3 3.35

Following trypsin treatment of a control (untreated) and TFEC-modified protein, the peptide mixture was analyzed on-line on a LTQ FT mass spectrometer, as indicated in the text. TFEC-modified residues are highlighted in bold face.