Peptide mapping is the principal technique for confirming a protein’s primary structure (amino acid sequence). The protein is digested using a proteolytic enzyme and the resultant peptides are analyzed by liquid chromatography–mass spectrometry (LC-MS). Our peptide mapping method combines an efficient digestion strategy, ultra-high performance LC separation and high resolution MS for in-depth protein characterization.
Peptide mapping forms an important part of protein structure analysis as it also allows for the analytical characterization of a variety of post-translational modifications (PTMs), including: deamidation, oxidation, N-terminal pyroglutamic acid, C-terminal lysine clipping and glycosylation.
Disulfide Bridges and Free Thiols
Generally reduction of the disulfide bonds is performed prior to proteolysis to improve digestion efficiency and maximize sequence coverage. Peptide mapping can also be performed without reduction to determine the positions of disulfide bridges and/or free thiols (sulfhydryl groups).
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