Top-down proteomics
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Top-down proteomics is a method of protein identification that uses an ion trapping mass spectrometer to store an isolated protein ion for mass measurement and tandem mass spectrometry analysis.[1][1] The name is derived from the similar approach to DNA seqencing.[1] Proteins are typically ionized by electrospray ionization and trapped in a Fourier transform ion cyclotron resonance (Penning trap)[1] or quadrupole ion trap (Paul trap) mass spectrometer. Fragmentation for tandem mass spectrometry is accomplished by electron capture dissociation or electron transfer dissociation.
See also
References
Bibliography
- Borchers CH, Thapar R, Petrotchenko EV, et al (2006). "Combined top-down and bottom-up proteomics identifies a phosphorylation site in stem-loop-binding proteins that contributes to high-affinity RNA binding". Proc. Natl. Acad. Sci. U.S.A. 103 (9): 3094–9. doi:10.1073/pnas.0511289103. PMID 16492733.
- Han X, Jin M, Breuker K, McLafferty FW (2006). "Extending top-down mass spectrometry to proteins with masses greater than 200 kilodaltons". Science 314 (5796): 109–12. doi:10.1126/science.1128868. PMID 17023655.
- Whitelegge J, Halgand F, Souda P, Zabrouskov V (2006). "Top-down mass spectrometry of integral membrane proteins". Expert review of proteomics 3 (6): 585–96. doi:10.1586/14789450.3.6.585. PMID 17181473.
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