Principle of Peptide Sequence Determination by Tandem Mass Spectrometry

Peptide sequencing involves detecting and analyzing the types and order of amino acids in the primary structure of peptides. Tandem mass spectrometry is commonly used for determining peptide sequences. Tandem mass spectrometry can directly determine the amino acid sequence of a peptide. The principle involves the generation of metastable ions during the ionization of peptides. By analyzing the mass differences between adjacent peaks of the same type, corresponding amino acid residues are identified.

In tandem mass spectrometry for peptide sequencing, primary mass spectrometry detects the parent ions of peptides, and those with higher mass peaks are selected to enter secondary mass spectrometry. After the parent ions enter secondary mass spectrometry, they undergo collision-induced dissociation with inert gases, resulting in fragment ion signals. By detecting these fragment ion signals, a secondary mass spectrum of the peptide is obtained. By analyzing the mass differences of the peptide fragments in the spectrum, the amino acid sequence of the peptide is deduced. The complete protein sequence can be determined by assembling the sequences of individual peptides.

Biotech company Biotyper offers peptide sequencing services using the Obitrap Fusion Lumos mass spectrometer from Thermo Fisher, combined with Nano-LC nanoliter chromatography technology.peptide sequencingThe Obitrap Fusion Lumos mass spectrometer is currently one of the highest resolution and sensitivity mass spectrometers, ensuring the sensitivity of low-abundance peptide fragment identification. During peptide fragmentation, a combination of HCD and ETD modes is used to ensure the integrity of peptide fragments. Once raw mass spectrometry data is obtained, we analyze it using database searches or de novo sequencing methods.

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