Protein mass spectrometry refers to the application of mass spectrometry to the study of proteins. Mass spectrometry is an important method for the accurate mass determination and characterization of proteins, and a variety of methods and instrumentations have been developed for its many uses. Its applications include the identification of proteins and their post-translational modifications, the elucidation of protein complexes, their subunits and functional interactions, as well as the global measurement of proteins in proteomics. It can also be used to localize proteins to the various organelles, and determine the interactions between different proteins as well as with membrane lipids.[1][2]
The two primary methods used for the ionization of protein in mass spectrometry are electrospray ionization (ESI) and matrix-assisted laser desorption/ionization (MALDI). These ionization techniques are used in conjunction with mass analyzers such as tandem mass spectrometry. In general, the proteins are analyzed either in a "top-down" approach in which proteins are analyzed intact, or a "bottom-up" approach in which protein are first digested into fragments. An intermediate "middle-down" approach in which larger peptide fragments are analyzed may also sometimes be used.
- ^ Jürgen Cox; Matthias Mann (July 2011). "Quantitative, High-Resolution Proteomics for Data-Driven Systems Biology". Annual Review of Biochemistry. 80: 273–299. doi:10.1146/annurev-biochem-061308-093216. PMID 21548781. – via Annual Reviews (subscription required)
- ^ Nelson P. Barrera; Carol V. Robinson (July 2011). "Advances in the Mass Spectrometry of Membrane Proteins: From Individual Proteins to Intact Complexes". Annual Review of Biochemistry. 80: 247–71. doi:10.1146/annurev-biochem-062309-093307. hdl:10533/135572. PMID 21548785. – via Annual Reviews (subscription required)