Tandem Fourier transform mass spectrometry

Tandem Fourier Transform Mass Spectrometry of Large Molecules... 

D. F. Hunt, J. Shabanowitz, R. T. Mclver, Jr., R. L. Hunter, and J. E. P. Syka, "Ionization and Mass Analysis of Nonvolatile Compounds by Particle Bombardment Tandem-Quadrupole Fourier Transform Mass Spectrometry," Anal. Chem., 57, 765-768 (1985). 

Mass spectrometry can also he used to obtain information about incompletely separated components. For e.xample, the mass spectrum of the front edge of a GC peak may be different from that of the middle part of the peak or the trailing edge if the peak is due lo more than one component. With mass spectrometry, we can not only determine that a peak is due to more than one species but also identify the various unresolved components. GO has also been coupled to tandem mass spectrometers or to Fourier transform mass spectrometers to give OC/MS/MS or GC/MS" sy.s-tems- These are extremely powerful tools for identifying components in mixtures. 

S. C. Beu, M. W. Senko, et al., Fourier transform electrospray instrumentation for tandem high-resolution mass spectrometry of large molecules, J. Am. Soc. Mass Spectrom. 4, 557-565 (1993). 

Laser-microprobe mass spectrometers are used for the study of solid surfaces. Ablation of the surface is accomplished with a high-power, pulsed laser, usually a Nd-YAG laser. After frequency quadrupling, theNd-YAG laser can produce 266-nm radiation focused to a spot as small as 0.5 pm. The power density of the radiation within this spot can be as high as 10to 10" W/cm. On ablation of the surface a small fraction of the atoms are ionized. The ions produced are accel crated and then analyzed, usually by tlme-of-flight mass spectrometry. In some cases laser microprobes have been combined with quadrupole ion traps and with Fourier transform mass spectrometers. Laser-microprobe tandem mass spectrometry is also receiv-... 

Chalmers, M. J. Hakansson, K. Johnson, R. Smith, R. Shen, j. Emmett, M. R. Marshall, A. G. Protein kinase A phosphorylation characterized by tandem Fourier transform ion cyclotron resonance mass spectrometry. Proteomics 2004, 4, 970-981. 

An on-line chromatography/atmospheric pressure chemical ionization tandem mass spectrometry (LC-APCI/MS/MS) methods was developed for rapid screen of pharmacokinetics of different drugs, including 5 (98RCM1216). The electron impact mass spectrum of 5 and ethyl 9,10-difluoro-3-methyl-7-oxo-2,3-dihydro-7Ff-pyrido[l,2,3- fe]-l,4-benzoxazine-6-carboxylate was reported (97MI28). Electron impact/Fourier transform... 

See footnote cto Table3 LC/PB/MS = hquid chromatography/particle beam mass spectrometry LC/APcl/ESl-MS/MS = liquid chromtography/atmospheric pressure chemical ionization/electrospray ionization tandem mass spectrometry LC/FTIR = Fourier transform infrared LC/TSP-MS/MS = liquid chromatography/thermospray tandem mass spectrometry LC/TSP-MS = liquid chromatography/thermospray mass spectrometry. 

Tandem Mass Spectrometry Electrospray Ionization Fourier Transform -Antibody-Based Identification... 

Multiple mass analyzers exist that can perform tandem mass spectrometry. Some use a tandem-in-space configuration, such as the triple quadrupole mass analyzers illustrated (Fig.3.9). Others use a tandem-in-time configuration and include instruments such as ion-traps (ITMS) and Fourier transform ion cyclotron resonance mass spectrometry (FTICRMS or FTMS). A triple quadrupole mass spectrometer can only perform the tandem process once for an isolated precursor ion (e.g., MS/MS), but trapping or tandem-in-time instruments can perform repetitive tandem mass spectrometry (MS ), thus adding n 1 degrees of structural characterization and elucidation. When an ion-trap is combined with HPLC and photodiode array detection, the net result is a profiling tool that is a powerful tool for both metabolite profiling and metabolite identification. 

The development of mass spectrometric techniques, such as fast atom bombardment mass spectrometry (FAB-MS), ° ° Fourier transform ion cyclotron resonance mass spectrometry (FTICR-MS), ° and tandem mass spectrometry (MS"), ° allowed enantiodiscrimination of chiral ion-dipole complexes the gas phase. These techniques and others will be illustrated in detail in the next Section 3. 

The main spectrometric identification techniques employed are gas chromatography/mass spectrometry (GC/MS) (13), liquid chromatography/tandem mass spectrometry (LC/MS(/MS)) (14), nuclear magnetic resonance (NMR) (11), and/or gas chromatography/Fourier transform infrared spectroscopy (GC/FL1R) (15). Each of these spectrometric techniques provides a spectrum that is characteristic of a chemical. MS and NMR spectra provide (detailed) structural information (like a fingerprint ), whereas an FUR spectrum provides information on functional groups. 

D.B. Cooper, R.W. Read, C.M. Timperley, N.H. Williams and R.M. Black, Identification of iso- and n -propylphosphonates using liquid chromatography-tandem mass spectrometry and gas chromatography-Fourier transform infrared spectroscopy, J. Chromatogr. A, 1040, 83-95 (2004). 

Capillary Electrophoresis Chemical Warfare Agents Chemical Weapons Convention Deuterated L-Alanine Triglycine Sulfate Dimethyl Ethylphosphonate Dimethyl Isopropylphosphonate Dimethyl Methylphosphonate Dimethyl Propylphosphonate Dimercaptotoluene Diffuse Reflectance Infrared Fourier Transform Functional Group Chromatograms Flame-Ionization Detector Fourier Transform Infrared Spectroscopy Gas Chromatography Gas Chromatography/Chemical Ionization/Mass Spectrometry Gas Chromatography/Chemical Ionization/Tandem Mass Spectrometry... 

To benefit general readers, the discussion has been limited to methodologies that are accessible to nonspecialists and that can be carried out on commercially available spectrometers without special modifications. The chapter illustrates the principles of mass spectrometry by demonstrating how various techniques [MALDI, ESI, Fourier transform ion cyclotron resonance (FT-ICR), ion traps, and tandem mass spectrometry (MS-MS)] work. It also provides examples of utilizing mass spectrometry to solve biological and biochemical problems in the field of protein analysis, protein folding, and noncovalent interactions of protein-DNA complexes. 

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