Protein Mass Spectrometry

Protein mass spectrometry is widely used to analyze biological samples for biomarker discovery, proteomics research, and clinical applications. Compared to other techniques used for the large-scale characterization of proteins, mass spectrometry has become a primary tool for proteomics based on its amenability to complex analysis. 

Mass spectrometry is used to quantitatively identify and characterize proteins based on their structure, post-translational modifications, and interactions.  

• Protein identification typically involves chemical or enzymatic digestion of proteins into peptides, which are then analyzed by mass spectrometry and identified using computational methods or sequencing.
• Post-translational modifications can be identified through changes in amino acid residue mass. Sites of modification can be mapped using sequencing or computational methods.
• For glycan analysis and profiling, enzymatic or chemical methods are used to release glycan moieties from glycoproteins, followed by derivatization of released glycans for mass spec analysis.
• Protein interactions are determined by affinity co-purification of a specific target protein with any interacting proteins or studied more globally using size exclusion or ion exchange chromatography prior to analysis by mass spectrometry.