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. Author manuscript; available in PMC: 2014 Oct 8.
Published in final edited form as: J Proteomics. 2013 Jun 24;91:10.1016/j.jprot.2013.06.021. doi: 10.1016/j.jprot.2013.06.021

Table 2.

Tryptic peptides of CHH identified by bottom-up de novo sequencing method.

Exptl MW Calcd MW Sequence a Tryptic peptide MS/MS spectrum b
1543.50 1543.71 AVFDQSCKGVYDR CHH[1-13] Fig. S7
2075.66 2076.01 AVFDQSCKGVYDRSLFGK CHH[1-18]
934.36 934.52 SLFGKLDR CHH[14-21] Fig. 7C
2420.79 2421.15 SLFGKLDRVCDDCYNLYRK CHH[14-32]
1760.49 1760.76 LDRVCDDCYNLYR CHH[19-31] Fig. S7
1888.53 1888.85 LDRVCDDCYNLYRK CHH[19-32]
1376.35 1376.55 VCDDCYNLYR CHH[22-31] Fig. S7
1504.39 1504.64 VCDDCYNLYRK CHH[22-32] Fig. S7
2358.16 2358.15 KHYVSTGCRKNCYGNLVFR CHH[32-50]
2230.06 2230.05 HYVSTGCRKNCYGNLVFR CHH[33-50] Fig. 7B
1269.64 1269.63 KNCYGNLVFR CHH[41-50] Fig. 7D
1141.35 1141.53 NCYGNLVFR CHH[42-50] Fig. S7
a

Fixed carbamidomethyl modification is on cysteine. The residues different from the homologous sequence are highlighted with underline.

b

Data is selectively shown for covering the sequence CHH[1-50]. CHH[51-71] was determined by top-down de novo sequencing.