Mass Spectrometry of Proteins and Peptides
- 3k Downloads
In the last few years, mass spectrometry (MS) has emerged as a major tool for the identification and characterization of peptides and proteins. It is now possible to measure proteins of masses > 100 kDa to an accuracy of a few Da, and to measure the masses of peptides with an accuracy of a few mDa. As a result, the information yielded by an MS measurement is highly specific. In addition, MS has extremely high sensitivity, often in the femtomole (10−15 mole) range, so it is a method that is suitable for the analysis of trace amounts of sample.
Mass spectrometry relies on the properties of charged particles moving under the influence of electric and magnetic fields, so the species studied must be ions (charge ze) rather than molecules. Most MS experiments are performed on positive ions, which can be formed either by the removal of one or more electrons from each molecule, or by the addition of one or more cations, usually protons. Consequently, the first step in any mass...
KeywordsQuadrupole Mass Filter Magnetic Sector Mass Spectrometer Pulse Laser Fire Linear Quadrupole Mass Filter Symmetric Electrostatic Field
- 1.McClosky JA (ed) (1990) Methods in enzymology, vol. 193: mass spectrometry. Academic Press, New York, N.Y. pp. 1–960Google Scholar
- 2.Cotter RJ (1997) Time-of-flight mass spectrometry: instrumentation and applications in biological research. American Chemical SocietyGoogle Scholar
- 12.Yost RA, Boyd RK (1990) Tandem mass spectrometry: quadrupole and hybrid instruments. In: (McClosky JA (ed) Methods in enzymology, vol. 193: mass spectrometry. Academic Press, New York, NY, pp 154–200Google Scholar
- 14.Ens W, Standing KG (2005) Hybrid quadrupole time-of-flight mass spectrometers for analysis of biomolecules. In: Burlingame AL (ed) Methods in enzymology, vol. 402: biological mass spectrometry. pp 49–78Google Scholar
- 16.Vestal ML, Campbell JM (2005) Tandem time-of-flight mass spectrometry. In: Burlingame AL (ed) Methods in enzymology, vol. 402: biological mass spectrometry. pp. 79–108Google Scholar
- 17.Jebanathirajah JA, Pittman JL, Thomson BA, Budnik BA, Kaur P, Rape M, Kirschner M, Costello CE, O'Connor PB (2005). Characterization of a new qQq-FTICR mass spectrometer for post-translational modification analysis and top-down tandem mass spectrometry of whole proteins. J Am Soc Mass Spectrom 16:1985–1999PubMedCrossRefGoogle Scholar