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Top-down proteomics

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]^[2] The name is derived from the similar approach to DNA seqencing.^[3] Proteins are typically ionized by electrospray ionization and trapped in a Fourier transform ion cyclotron resonance (Penning trap)^[4] or quadrupole ion trap (Paul trap) mass spectrometer. Fragmentation for tandem mass spectrometry is accomplished by electron capture dissociation or electron transfer dissociation.

References

^ Sze SK, Ge Y, Oh H, McLafferty FW (2002). "Top-down mass spectrometry of a 29-kDa protein for characterization of any posttranslational modification to within one residue". Proc. Natl. Acad. Sci. U.S.A. 99 (4): 1774–9. doi:10.1073/pnas.251691898. PMID 11842225.
^ Kelleher NL (2004). "Top-down proteomics". Anal. Chem. 76 (11): 197A–203A. PMID 15190879.
^ Smith CL, Cantor CR (1989). "Evolving strategies for making physical maps of mammalian chromosomes". Genome 31 (2): 1055–8. PMID 2698822.
^ Bogdanov B, Smith RD (2005). "Proteomics by FTICR mass spectrometry: top down and bottom up". Mass spectrometry reviews 24 (2): 168–200. doi:10.1002/mas.20015. PMID 15389855.

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.