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.
Deepalakshmi
Putchen Dakshinamoorthy
PD
Mass Spectrometry Facility, National Centre for Biological Sciences-TIFR, GKVK PO, Bellary Road, Bangalore 560 065, India. deepalakshmi@ncbs.res.in
D000465:Algorithms; D000595:Amino Acid Sequence; D008969:Molecular Sequence Data; D008970:Molecular Weight; D023302:Protein Footprinting / Q000379:methods*; D011994:Recombinant Proteins / Q000737:chemistry*; D020539:Sequence Analysis, Protein / Q000379:methods*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / Q000379:methods*
D011994:Recombinant Proteins