C-terminal Sequencing of Proteins

Protein sequencing is the identification of the types of amino acids in a protein and the analysis of their arrangement. C-terminal protein sequencing refers to the detection and analysis of the amino acid sequence of the primary structure of the protein's C-terminus. The Edman degradation method used for N-terminal sequencing cannot be used for determining C-terminal sequences. Instead, tandem mass spectrometry is commonly used for C-terminal protein sequencing. Mass spectrometry-based C-terminal protein sequencing involves enzymatically cleaving the sample protein with trypsin before directly introducing the peptide mixture into mass spectrometry for detection. The enzymatically digested protein peptides are collected in the first stage of mass spectrometry (Q1) to gather C-terminal peptide ion signals, which then undergo systematic collision-induced fragmentation in the second stage of mass spectrometry (Q2). The resulting peptide fragment ion signals are captured to obtain the peptide mass spectrum, which can be analyzed to confirm the C-terminal sequence information of the protein peptide.

Biotech company Biotech-Pack uses Thermo's Obitrap Fusion Lumos mass spectrometer to develop a mass spectrometry-basedprotein N/C-terminal sequencingtechnology to achieve sequence analysis of protein samples. The Obitrap Fusion Lumos mass spectrometer is currently the highest in resolution and sensitivity, ensuring the sensitivity of low-abundance peptide fragment identification. During the peptide fragmentation process, a combination of HCD and ETD modes is used to ensure the integrity of peptide fragments. This allows for N-terminal, C-terminal, and full-length sequence analysis of protein samples.

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