Can mass spectrometry detect types of protein modifications?
Mass spectrometry (MS) can be used to detect and quantify proteins in biological samples as well as their modifications. In mass spectra, the mass-to-charge ratio of modified peptides shows a significant difference compared to unmodified peptides. By analyzing these differences, not only can the modification sites on peptides be determined, but the type and quantity of modifications can also be inferred.
Common protein modifications include phosphorylation (increase of 80 Da), acetylation (increase of 42 Da), methylation (increase of 14 Da), etc. Protein samples are digested by enzymes, separated by chromatography, and ionized before being sent to a mass spectrometer. The speed of movement of these proteins or peptides in an electric field depends on their mass-to-charge ratio, which allows the determination of their mass/charge values. Modifications typically change the mass of proteins, and these small mass changes can be detected by mass spectrometry.
Specific analytical methods, data interpretation, and utilizing this information to understand protein function generally require specialized software and complex data analysis techniques. This is a field that demands specialized knowledge and experience.
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