Can Mass Spectrometry Detect Types of Protein Modifications

Mass spectrometry (MS) is a powerful technique for detecting and quantifying proteins and their post-translational modifications in biological samples. In mass spectra, modified peptides exhibit distinct mass-to-charge ratios compared to their unmodified counterparts. Analyzing these differences allows for the identification of modification sites and enables the inference of both the type and extent of modifications.

 

Common protein modifications include phosphorylation (an increase of 80 Da), acetylation (an increase of 42 Da), and methylation (an increase of 14 Da). Protein samples are typically subjected to enzymatic digestion, chromatographic separation, and ionization before being analyzed by a mass spectrometer. The velocity of proteins or peptides in an electric field is determined by their mass-to-charge ratios, allowing for the precise measurement of their mass/charge values. Subtle mass variations due to protein modifications can be sensitively detected using mass spectrometry.

 

Specialized software and advanced data analysis techniques are often required to interpret these data and utilize the information to elucidate protein functions. This field necessitates specialized knowledge and expertise.

 

MtoZ Biolabs, an integrated chromatography and mass spectrometry (MS) services provider.

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