Top-down approach of completely sequencing a 4.9 kDa recombinant peptide using quadrupole time-of-flight mass spectrometry.

A recombinant peptide (near the C-terminal region of head involution defective protein) of 4.9 kDa has been completely sequenced and characterized using medium-resolution mass spectrometry (QTOF). The observed difference in the experimental mass and the theoretical mass is due to beta-mercaptoethanol adduct formation on the cysteine residue. The fragmentation pattern is correlated with the primary structure of the protein. Top-down sequencing of the peptide was extended to small proteins like barstar of mass 10.3 kDa.