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Tandem mass spectrometry, also known as MS/MS or MS2, is a technique in instrumental analysis where two or more mass analyzers are coupled together using an additional reaction step to increase their abilities to analyse chemical samples. A common use of tandem MS is the analysis of biomolecules, such as proteins and peptides.
Fourier-transform ion cyclotron resonance mass spectrometry is a type of mass analyzer for determining the mass-to-charge ratio (m/z) of ions based on the cyclotron frequency of the ions in a fixed magnetic field. The ions are trapped in a Penning trap, where they are excited to a larger cyclotron radius by an oscillating electric field orthogonal to the magnetic field. After the excitation field is removed, the ions are rotating at their cyclotron frequency in phase. These ions induce a charge on a pair of electrodes as the packets of ions pass close to them. The resulting signal is called a free induction decay (FID), transient or interferogram that consists of a superposition of sine waves. The useful signal is extracted from this data by performing a Fourier transform to give a mass spectrum.
Infrared multiple photon dissociation (IRMPD) is a technique used in mass spectrometry to fragment molecules in the gas phase usually for structural analysis of the original (parent) molecule.
Electron-capture dissociation (ECD) is a method of fragmenting gas-phase ions for structure elucidation of peptides and proteins in tandem mass spectrometry. It is one of the most widely used techniques for activation and dissociation of mass selected precursor ion in MS/MS. It involves the direct introduction of low-energy electrons to trapped gas-phase ions.
The history of mass spectrometry has its roots in physical and chemical studies regarding the nature of matter. The study of gas discharges in the mid 19th century led to the discovery of anode and cathode rays, which turned out to be positive ions and electrons. Improved capabilities in the separation of these positive ions enabled the discovery of stable isotopes of the elements. The first such discovery was with the element neon, which was shown by mass spectrometry to have at least two stable isotopes: 20Ne and 22Ne. Mass spectrometers were used in the Manhattan Project for the separation of isotopes of uranium necessary to create the atomic bomb.
Surface-enhanced laser desorption/ionization (SELDI) is a soft ionization method in mass spectrometry (MS) used for the analysis of protein mixtures. It is a variation of matrix-assisted laser desorption/ionization (MALDI). In MALDI, the sample is mixed with a matrix material and applied to a metal plate before irradiation by a laser, whereas in SELDI, proteins of interest in a sample become bound to a surface before MS analysis. The sample surface is a key component in the purification, desorption, and ionization of the sample. SELDI is typically used with time-of-flight (TOF) mass spectrometers and is used to detect proteins in tissue samples, blood, urine, or other clinical samples, however, SELDI technology can potentially be used in any application by simply modifying the sample surface.
Electron-transfer dissociation (ETD) is a method of fragmenting multiply-charged gaseous macromolecules in a mass spectrometer between the stages of tandem mass spectrometry (MS/MS). Similar to electron-capture dissociation, ETD induces fragmentation of large, multiply-charged cations by transferring electrons to them. ETD is used extensively with polymers and biological molecules such as proteins and peptides for sequence analysis. Transferring an electron causes peptide backbone cleavage into c- and z-ions while leaving labile post translational modifications (PTM) intact. The technique only works well for higher charge state peptide or polymer ions (z>2). However, relative to collision-induced dissociation (CID), ETD is advantageous for the fragmentation of longer peptides or even entire proteins. This makes the technique important for top-down proteomics. The method was developed by Hunt and coworkers at the University of Virginia.
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.
Top-down proteomics is a method of protein identification that either uses an ion trapping mass spectrometer to store an isolated protein ion for mass measurement and tandem mass spectrometry (MS/MS) analysis or other protein purification methods such as two-dimensional gel electrophoresis in conjunction with MS/MS. Top-down proteomics is capable of identifying and quantitating unique proteoforms through the analysis of intact proteins. The name is derived from the similar approach to DNA sequencing. During mass spectrometry intact proteins are typically ionized by electrospray ionization and trapped in a Fourier transform ion cyclotron resonance, quadrupole ion trap or Orbitrap mass spectrometer. Fragmentation for tandem mass spectrometry is accomplished by electron-capture dissociation or electron-transfer dissociation. Effective fractionation is critical for sample handling before mass-spectrometry-based proteomics. Proteome analysis routinely involves digesting intact proteins followed by inferred protein identification using mass spectrometry (MS). Top-down MS (non-gel) proteomics interrogates protein structure through measurement of an intact mass followed by direct ion dissociation in the gas phase.
Fred Warren McLafferty was an American chemist known for his work in mass spectrometry. He is best known for the McLafferty rearrangement reaction that was observed with mass spectrometry. With Roland Gohlke, he pioneered the technique of gas chromatography–mass spectrometry. He is also known for electron-capture dissociation, a method of fragmenting gas-phase ions.
The Scottish Instrumentation and Research Centre for Advanced Mass Spectrometry (SIRCAMS) is a facility for ultra-high resolution mass spectrometry of biomolecules. SIRCAMS is based in the University of Edinburgh School of Chemistry.
Electron capture ionization is the ionization of a gas phase atom or molecule by attachment of an electron to create an ion of the form . The reaction is
In mass spectrometry, fragmentation is the dissociation of energetically unstable molecular ions formed from passing the molecules in the ionization chamber of a mass spectrometer. The fragments of a molecule cause a unique pattern in the mass spectrum. These reactions are well documented over the decades and fragmentation pattern is useful to determine the molar weight and structural information of the unknown molecule. Fragmentation that occurs in tandem mass spectrometry experiments has been a recent focus of research, because this data helps facilitate the identification of molecules.
Neil L. Kelleher is the Walter and Mary Elizabeth Glass Professor of Chemistry, Molecular Biosciences, and Medicine at Northwestern University. His research focuses on mass spectrometry, primarily its application to proteomics. He is known mainly for top-down proteomics and the development of the fragmentation technique of electron-capture dissociation with Roman Zubarev while in Fred McLafferty's lab at Cornell University.
The isotopic resonance hypothesis(IsoRes) postulates that certain isotopic compositions of chemical elements affect kinetics of chemical reactions involving molecules built of these elements. The isotopic compositions for which this effect is predicted are called resonance isotopic compositions.
Kristina Håkansson is an analytical chemist known for her contribution in Fourier transform ion cyclotron resonance (FT-ICR) mass spectrometry for biomolecular identification and structural characterization. Currently, she holds the position of Professor of Chemistry at University of Michigan. Her research focuses on mass spectrometry, primarily identification and characterization of protein posttranslational modifications by complementary fragmentation techniques such as electron-capture dissociation (ECD)/negative ion ECD (niECD) and infrared multiphoton dissociation (IRMPD) at low (femtomole) levels.
The Biemann Medal is awarded annually by the American Society for Mass Spectrometry (ASMS) to an individual early in his or her career in recognition of significant achievement in basic or applied mass spectrometry. It is named after professor Klaus Biemann.
Viatcheslav (“Slava”) Borisovich Artaev is a Russian-American physicist who studies Mass Spectrometry technology. He currently works as the Technical Director for Research and Development of the Separation Science Division for LECO Corporation based in Saint Joseph, Michigan, USA.:
Ying Ge is a Chinese-American biologist who is a Professor of Cell and Regenerative Biology at the University of Wisconsin–Madison. Her research considers the molecular mechanisms that underpin cardiac disease. She has previously served on the board of directors of the American Society for Mass Spectrometry. In 2020 Ge was named on the Analytical Scientist Power List.
References
- ↑ Zubarev, R. A.; Kelleher, N. L.; McLafferty, F. W. Electron Capture Dissociation of Multiply Charged Protein Cations. A Non-ergodic Process, J. Am. Chem. Soc. 1998, 120, 3265-3266.
- ↑ Zubarev, R. A.; Artemenko, K. A.; Zubarev, A. R.; Mayrhofer, C.; Yang, H.; Fung, E. Y. M. Early life relict feature in peptide mass distribution, Cent. Eur. J. Biol.2010,5, 190-196.
- ↑ Xie, X.; Zubarev, R. A. Isotopic Resonance Hypothesis: Experimental Verification by Escherichia coli Growth Measurements, Scientific Reports, 2015, doi:10.1038/srep09215
- ↑ Johnson, B. A.; Shirokawa, J. M.; Geddes, J. W.; Choid, B. H.; Kim, R. C.; Aswad, D. W. Protein L-isoaspartyl methyltransferase in postmortem brains of aged humans, Neurobiology of Aging, 1991, 12, 19-24.
- ↑ Yang, H.; Lyutvinskiy, Y.; Herukka, S.-K.; Soininen, H.; Rutishauser, D.; Zubarev, R. A. Prognostic polypeptide blood plasma biomarkers of Alzheimer’s disease progression,J Alzheimer’s Disease,2014,40, 659-66.
- ↑ Xie, X.; Backman, D.; Lebedev, A. T.; Artaev, V. B.; Jiang, L.; Ilag, L. L.; Zubarev, R. A. Primordial soup was edible: abiotically produced Miller-Urey mixture supports bacterial growth,Scientific Reports,2015, 5, article number: 14338, doi:10.1038/srep14338
- ↑ Bernadotte, A.; Semenova, V.; Musial, V. A. M.; Kasprzykowska, A.; Zubarev, R. A. Self-assembly of Deinococcus radiodurans supports nanocell scenario of life origin, Discoveries,2017, 5, E72, doi: 10.15190/d.2017.2.
- ↑ Brodbelt JS, McLafferty FW, Kelleher NL (2008). "Focus in honor of Roman Zubarev, recipient of the 2007 Biemann Medal". J. Am. Soc. Mass Spectrom. 19 (6): 751–2. doi: 10.1016/j.jasms.2008.04.021 . PMID 18499035.