Mass Change of Peptides After Fragmentation in Mass Spectrometry
1. Peptide Fragmentation in Mass Spectrometry
Mass spectrometry is a commonly used analytical technique that determines the mass spectrum of a substance by measuring the mass-to-charge ratio of particles, creating a map or spectrum. In protein mass spectrometry, peptides are generated through fragmentation, usually achieved via collision-induced dissociation or electron capture dissociation. Once peptides are fragmented in the mass spectrometer, they produce a series of ions with specific masses. These mass changes offer valuable information about the sequence of the original peptide.
2. Analysis of Mass Changes
Measuring the mass of ions from fragmented peptides provides important information regarding the fragmentation process. From this information, we can deduce the amino acid sequence of the original peptide and any potential post-translational modifications. Since the masses of amino acids are known, by comparing the mass changes of the fragmented ions with known amino acid masses, we can infer the amino acid sequence of the peptide. If there is a discrepancy between the theoretical and actual measured mass, it may indicate the presence of post-translational modifications, such as phosphorylation or acetylation.
3. Importance and Applications
Analyzing the mass changes of peptides after fragmentation in mass spectrometry not only helps us understand the structure and function of proteins but also finds applications in biomedical research. For instance, by analyzing the changes in peptide mass, disease biomarkers can be identified, which is crucial for disease diagnosis and monitoring therapeutic efficacy. Additionally, it enables the identification of new disease-related proteins or the study of functional changes in proteins during disease processes.
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