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Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'Mass spectrometry.'
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Journal articles on the topic "Mass spectrometry":
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KASAMA, Takeshi. "Biological Mass Spectrometry. Quadrupole Mass Spectrometer." Journal of the Mass Spectrometry Society of Japan 44, no. 3 (1996): 393–405. http://dx.doi.org/10.5702/massspec.44.393.
Glish, Gary L., and David J. Burinsky. "Hybrid mass spectrometers for tandem mass spectrometry." Journal of the American Society for Mass Spectrometry 19, no. 2 (February 2008): 161–72. http://dx.doi.org/10.1016/j.jasms.2007.11.013.
Busch, Kenneth L., Gary L. Glish, Scott A. McLuckey, and John J. Monaghan. "Mass spectrometry/mass spectrometry: techniques and applications of tandem mass spectrometry." Analytica Chimica Acta 237 (1990): 509. http://dx.doi.org/10.1016/s0003-2670(00)83956-2.
Futrell, Jean H. "Mass spectrometry/mass spectrometry: Techniques and applications of tandem mass spectrometry." Microchemical Journal 41, no. 2 (April 1990): 246–47. http://dx.doi.org/10.1016/0026-265x(90)90124-n.
Moriarty, F. "Mass spectrometry/mass spectrometry. Techniques and applications of tandem mass spectrometry." Environmental Pollution 61, no. 3 (1989): 261. http://dx.doi.org/10.1016/0269-7491(89)90246-7.
Cooks, R. G. "Mass Spectrometry/Mass Spectrometry. Techniques and Applications of Tandem Mass Spectrometry." International Journal of Mass Spectrometry and Ion Processes 93, no. 2 (October 1989): 265–66. http://dx.doi.org/10.1016/0168-1176(89)80103-x.
Pinkston, J. David, Martin Rabb, J. Throck Watson, and John Allison. "New time‐of‐flight mass spectrometer for improved mass resolution, versatility, and mass spectrometry/mass spectrometry studies." Review of Scientific Instruments 57, no. 4 (April 1986): 583–92. http://dx.doi.org/10.1063/1.1138874.
Glish, Gary L., and Scott A. McLuckey. "Hybrid Instruments for Mass Spectrometry/Mass Spectrometry." Instrumentation Science & Technology 15, no. 1 (January 1986): 1–36. http://dx.doi.org/10.1080/10739148608543593.
Charles, M. Judith, and Yves Tondeur. "Choosing between high-resolution mass spectrometry and mass spectrometry/mass spectrometry environmental applications." Environmental Science & Technology 24, no. 12 (December 1990): 1856–60. http://dx.doi.org/10.1021/es00082a011.
KONDO, Fumio, and Ken-ichi HARADA. "Biological Mass Spectrometry. Mass Spectrometric Analysis of Cyanobacterial Toxins." Journal of the Mass Spectrometry Society of Japan 44, no. 3 (1996): 355–76. http://dx.doi.org/10.5702/massspec.44.355.
Dissertations / Theses on the topic "Mass spectrometry":
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Lemire, Sharon Warford. "Rigorous analytical applications of liquid secondary ion mass spectrometry/mass spectrometry." Diss., Georgia Institute of Technology, 1996. http://hdl.handle.net/1853/30026.
Dabney, David E. "Analysis of Synthetic Polymers by Mass Spectrometry and Tandem Mass Spectrometry." University of Akron / OhioLINK, 2009. http://rave.ohiolink.edu/etdc/view?acc_num=akron1259021862.
Goodwin, Lee. "Capillary electrophoresis-mass spectrometry and tandem mass spectrometry studies of ionic agrochemicals." Thesis, University of York, 2003. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.398906.
Shliaha, Pavel Vyacheslavovich. "Investigation of protein abundance and localization by mass spectrometry and ion-mobility spectrometry-mass spectrometry methods." Thesis, University of Cambridge, 2015. https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.708661.
Hsi, Kuang-Ying. "Peptide identification of tandem mass spectrometry from quadrupole time-of-flight mass spectrometers." Diss., [La Jolla] : University of California, San Diego, 2009. http://wwwlib.umi.com/cr/ucsd/fullcit?p1462246.
Thesis (M.S.)--University of California, San Diego, 2009. Title from first page of PDF file (viewed May 4, 2009). Available via ProQuest Digital Dissertations. Includes bibliographical references (p. 45-46).
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Yuen, Wei Hao. "Ion imaging mass spectrometry." Thesis, University of Oxford, 2012. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.564395.
This work investigates the applicability of fast detectors to the technique of microscope-mode imaging mass spectrometry. By ionising analyte from a large area of the sample, and projecting the desorbed ions by the use of ion optics through a time-of-flight mass spectrometer onto a two- dimensional detector, time- (and hence mass-) dependent distributions of ions may be imaged. To date, this method of imaging mass spectrometry has been limited by the ability to image only one mass window of interest per experimental cycle, limiting throughput and processing speed. Thus, the alternative microprobe-mode imaging mass spectrometry is currently the dominant method of analysis, with its superior mass resolution. The application of fast detectors to microscope-mode imaging lifts the restriction of the detection of a single mass window per experimental cycle, potentially decreasing acquisition time by a factor of the number of mass peaks of interest. Additional advantages include the reduction of sample damage by laser ablation, and the potential identification of coincident eo-fragments of different masses originating from the same parent molecule. Theoretical calculations and simulations have been performed confirming the suitability of conventional time-of-flight velocity-mapped ion imaging apparatus for imaging mass spectrometry. Only small modifications to the repeller plate and laser beam path, together with the adjustment of the accelerating potential field, were required to convert the apparatus to a wide (7 mm diameter) field-of-view ion microscope. Factors affecting the mass and spatial resolution were investigated with these theoretical calculations, with theoretical calculations predicting a spatial resolution of about 26μm and m/m of 93. Typical experimental data collected from velocity-mapped ion imaging experiments were collected, and characterised in order to provide specifications for a novel time-stamping detector, the Pixel Imaging Mass Spectrometry detector. From these data, the suitability of thresholding and centroiding on the new detector was determined. Initial experiments using desorptionjionisation on silicon and conventional charge-coupled device cameras confirmed the correct spatial-mapping of the apparatus. Matrix-assisted laser desorptionjionisation techniques (MALDI) were used in experiments to determine the spatial and mass resolutions attainable with the apparatus. Experimental spatial resolutions of 14.4 μm and m/m of 60 were found. The better experimental spatial resolution indicates a higher di- rectionality of initial velocities from MALDI desorption than used in the theoretical predictions, while the poorer mass resolution could be attributed to limitations imposed by the use of the phosphor screen. Proof-of-concept experiments using fast-framing cameras and the new time-stamping detectors confirmed the feasibility of multiple mass acquisition in time-of-flight microscope mode ion imaging. Mass-dependent distributions were acquired of different pigment distributions in each experimental cycle. Finally, spatial-mapped images of coronal mouse brain sections were acquired using both conventional and fast detectors. The apparatus was demonstrated to provide accurate spatial distributions with a wide field-of-view, and multiple mass distributions were acquired with each experimental cycle using the new time-stamping detector.
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Berezovskaya, Yana. "Investigation of protein-ion interactions by mass spectrometry and ion mobility mass spectrometry." Thesis, University of Edinburgh, 2012. http://hdl.handle.net/1842/7747.
Protein‐ion interactions play an important role in biological systems. A considerable number of elements (estimated 25 – 30) are essential in higher life forms such as animals and humans, where they are integral part of enzymes involved in plethora of cellular processes. It is difficult to overestimate the importance of thorough understanding of how protein‐ion interplay affects living cell in order to be able to address therapeutic challenges facing humanity. Presented to the reader’s attention is a gas‐phase biophysical analysis of peptides’ and proteins’ interactions with biologically relevant ions (Zn2+ and I–). This investigation provides an insight into conformational changes of peptides and proteins triggered by ions. Mass spectrometry and ion mobility mass spectrometry are used in this work to probe peptide and protein affinities for a range of ions, along with conformational changes that take place as a result of binding. Observation of peptide and protein behaviour in the gas phase can inform the investigator about their behaviour in solution prior to ionisation and transfer from the former into the latter phase. Wherever relevant, the gas‐phase studies are complemented by molecular dynamics simulations and the results are compared to solution phase findings (spectroscopy). Two case studies of protein‐ion interactions are presented in this thesis. Firstly, sequence‐to‐structure relationships in proteins are considered via protein design approach using two synthetic peptide‐based systems. The first system is a synthetic consensus zinc finger sequence (vCP1) that is responsive to zinc: it adopts a zinc finger fold in the presence of Zn2+ by coordinating the metal ion by two cysteines and two histidines. This peptide has been selected as a reference for the zinc‐bound state and a simple model to refine the characterisation method in preparation for analysis of a more sophisticated second system – dual conformational switch. This second system (ZiCop) is designed to adopt either of the two conformations in response to a stimulus: zinc finger or coiled coil. The reversible switch between the two conformational states is controlled by the binding of zinc ion to the peptide. Interactions of both peptide systems with a number of other divalent metal cations (Co2+, Ca2+ and Cu2+) are considered also, and the differences in binding and switching behaviour are discussed. Secondly, protein‐salt interactions are investigated using three proteins (lysozyme, cytochrome c and BPTI) using variable temperature ion mobility mass spectrometry. Ion mobility measurements were carried out on these proteins with helium as the buffer gas at three different drift cell temperatures – ‘ambient’ (300 K), ‘cold’ (260 K) and ‘hot’ (360 K), and their conformational preferences in response to HI binding and temperature are discussed.
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Liu, Xiumin. "Mass Spectrometry and Tandem Mass Spectrometry Analysis of Polymers and Polymer-Protein Interactions." University of Akron / OhioLINK, 2014. http://rave.ohiolink.edu/etdc/view?acc_num=akron1406838246.
Kaleta, Erin. "Applications of mass spectrometry to bacterial diagnostics: Affinity capture matrix assisted laser desorption/ionization mass spectrometry and polymerase chain reaction mass spectrometry." Diss., The University of Arizona, 2011. http://hdl.handle.net/10150/305352.
This dissertation presents the application of mass spectrometry to the detection and characterization of microorganisms based on biomarker identification and DNA analysis. Two major topics are covered: affinity capture mass spectrometry using immunoassay methods and methods involving insertion of membrane receptors into polymerized planar supported lipid bilayers; and the application of mass spectrometry for use in clinical microbiology for the identification of microorganisms causing bloodstream infections.
Affinity capture mass spectrometry on immunoassay-based platforms studied the capture of Protein A from Staphylococcus aureus , demonstrating capture that is both selective and sensitive. Experiments illustrated successful capture from a purified source and cell lysates. Affinity capture using receptors inserted into polymerized lipid bilayers was also performed using GM1 and cholera toxin subunit B, demonstrating the enhanced stability offered by polymerizing the lipid bilayers such that direct ionization could be performed. Detection of protein binding was achieved with mass spectrometry at low molar ratios of receptor, and enzymatic digestion experiments on the protein retained at the surface illustrated the ability to characterize the protein ligand bound, lending support to using this technique for reverse pharmacological applications. Lastly, experiments demonstrated that affinity capture of surface-bound proteins can also be used to extract cells from complex mixture prior to the polymerase chain reaction, illustrating utility as a pre-treatment for detecting microorganisms in blood samples.
Mass spectrometry was applied to detection of microorganisms from blood culture bottles collected from patients with bloodstream infections. Polymerase chain reaction electrospray ionization and whole cell matrix-assisted laser desorption/ionization mass spectrometry were used to characterize hematopathogens. High diagnostic accuracy was demonstrated with respect to culture-based testing and these two platforms were compared considering accuracy in identification, time to result, and cost benefit analysis.
The experiments presented here cover a broad range of detection strategies for identifying proteins and microorganisms. The affinity capture techniques describe the first application of peptide capture and polymerized bilayers for mass spectrometric analysis, and the clinical mass spectrometry work demonstrates validation of two emerging techniques and the first comparative study on both platforms simultaneously. All research presented here demonstrates promise for application of mass spectrometry in diagnostic biology.
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Sun, Xiaobo. "Forensic Applications of Gas Chromatography/Mass Spectrometry, High Performance Liquid Chromatography--Mass Spectrometry and Desorption Electrospray Ionization Mass Spectrometry with Chemometric Analysis." Ohio University / OhioLINK, 2012. http://rave.ohiolink.edu/etdc/view?acc_num=ohiou1329517616.
Gross, Jürgen H. "Introduction." In Mass Spectrometry, 1–20. Berlin, Heidelberg: Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-642-10711-5_1.
Gross, Jürgen H. "Fast Atom Bombardment." In Mass Spectrometry, 479–506. Berlin, Heidelberg: Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-642-10711-5_10.
Gross, Jürgen H. "Matrix-Assisted Laser Desorption/Ionization." In Mass Spectrometry, 507–59. Berlin, Heidelberg: Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-642-10711-5_11.
Gross, Jürgen H. "Electrospray Ionization." In Mass Spectrometry, 561–620. Berlin, Heidelberg: Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-642-10711-5_12.
Gross, Jürgen H. "Ambient Mass Spectrometry." In Mass Spectrometry, 621–49. Berlin, Heidelberg: Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-642-10711-5_13.
Gross, Jürgen H. "Hyphenated Methods." In Mass Spectrometry, 651–84. Berlin, Heidelberg: Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-642-10711-5_14.
Gross, Jürgen H. "Inorganic Mass Spectrometry." In Mass Spectrometry, 685–716. Berlin, Heidelberg: Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-642-10711-5_15.
Gross, Jürgen H. "Principles of Ionization and Ion Dissociation." In Mass Spectrometry, 21–66. Berlin, Heidelberg: Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-642-10711-5_2.
Gross, Jürgen H. "Isotopic Composition and Accurate Mass." In Mass Spectrometry, 67–116. Berlin, Heidelberg: Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-642-10711-5_3.
Conference papers on the topic "Mass spectrometry":
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Travis, J. C., T. B. Lucatorto, J. Wen, J. D. Fassett, and C. W. Clark. "Doppler-Free Resonance Ionization Mass Spectrometry of Beryllium." In Laser Applications to Chemical Analysis. Washington, D.C.: Optica Publishing Group, 1987. http://dx.doi.org/10.1364/laca.1987.tub2.
As originally conceived, resonance ionization mass spectrometry (RIMS) combined the elemental selectivity of resonance ionization (1) with the isotopic selectivity of mass spectrometry to improve the accuracy and sensitivity of conventional mass spectrometry (2). For many applications, especially quantitation by isotope dilution (3) , it is important that no isotopic selectivity accompany the resonance ionization process. This condition is easily met for all but a few elements of the periodic table (4), since the great majority of optical isotope shifts are small with respect to typical dye laser bandwidths and Doppler-broadened linewidths in common atom reservoirs. However, another class of problem exists for which it is desirable to achieve isotopically selective resonance ionization. These applications involve the detection of extremely, rare stable or radioactive isotopes in the presence of the major isotopic species of an element. Miller et al. (5) have explored the optical isotopic selectivity of the isotopes of Lu using a RIMS spectrometer equipped with a high-resolution (single-mode) continuous-wave (cw) laser. Cannon et al. (6) have measured an optical selectivity (defined below) of 800 for isotopes of Ba, using a RIMS spectrometer with two cw lasers. We have proposed the use of pulsed, two-photon, Doppler-free resonance ionization to extend the capability of conventional mass spectrometers to measure isotope ratios in excess of 1012 (7). Initial experimental results using this approach, for the isotopes 9Be and 10Be, are reported here.
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Johnston, Murray V., and Patrick J. McKeown. "Rapid single-particle mass spectrometry." In OSA Annual Meeting. Washington, D.C.: Optica Publishing Group, 1992. http://dx.doi.org/10.1364/oam.1992.tuu3.
Single particles are detected on the fly by laser desorption mass spectrometry. Particles entering the source region of the mass spectrometer scatter radiation from a helium-neon laser beam. The scattered radiation triggers an excimer laser, causing one step laser desorption and ionization of the particle. A complete mass spectrum is subsequently recorded with a time-of-flight mass analyzer. Aerosols are sampled from atmospheric pressure through a two-stage differentially pumped inlet. Since the particle transit time in the vacuum prior to analysis is small, evaporation of volatile components is minimized. We have used rapid single-particle mass spectrometry to detect both inorganic and organic species.1 When a relatively low irradiance for laser desorption is used, incomplete ablation of the particle occurs and material located near the surface is preferentially sampled. Higher laser irradiances sample a greater fraction of the entire particle. Potential applications include the analysis of airborne particulate matter and the detection of trace species adsorbed to suspended microparticles in solution.
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Kim, J. C. "Accelerator mass spectrometry." In HADRONS AND NUCLEI: First International Symposium. AIP, 2001. http://dx.doi.org/10.1063/1.1425525.
Sarycheva, Anastasia, Anton Grigoryev, Evgeny N. Nikolaev, and Yury Kostyukevich. "Robust Simulation Of Imaging Mass Spectrometry Data." In 35th ECMS International Conference on Modelling and Simulation. ECMS, 2021. http://dx.doi.org/10.7148/2021-0192.
Mass spectrometry imaging (MSI) with high resolution in mass and space is an analytical method that produces distributions of ions on a sample surface. The algorithms for preprocessing and analysis of the raw data acquired from a mass spectrometer should be evaluated. To do that, the ion composition at every point of the sample should be known. This is possible via the employment of a simulated MSI dataset. In this work, we suggest a pipeline for a robust simulation of MSI datasets that resemble real data with an option to simulate the spectra acquired from any mass spectrometry instrument through the use of the experimental MSI datasets to extract simulation parameters.
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Downey, Stephen W. "Comparison of secondary ion mass spectrometry and resonance ionization mass spectrometry." In OE/LASE '90, 14-19 Jan., Los Angeles, CA, edited by Nicholas S. Nogar. SPIE, 1990. http://dx.doi.org/10.1117/12.17881.
Thompson, James K. "Ion Balance Mass Spectrometry." In ATOMIC PHYSICS 19: XIX International Conference on Atomic Physics; ICAP 2004. AIP, 2005. http://dx.doi.org/10.1063/1.1928840.
Campana, Joseph E. "Laser probe mass spectrometry." In Optics, Electro-Optics, and Laser Applications in Science and Engineering, edited by David D. Saperstein. SPIE, 1991. http://dx.doi.org/10.1117/12.45139.
Stepaniuk, Mykola, Stefano Nisi, and Marco Balata. "Hands on mass spectrometry." In Gran Sasso Summer Institute 2014 Hands-On Experimental Underground Physics at LNGS. Trieste, Italy: Sissa Medialab, 2015. http://dx.doi.org/10.22323/1.229.0026.
Kawai, Yosuke, Kentaro Terada, Toshinobu Hondo, Jun Aoki, Morio Ishihara, Michisato Toyoda, and Ryosuke Nakamura. "Development of a Secondary Neutral Mass Spectrometer for Submicron Imaging Mass Spectrometry." In Proceedings of the 15th International Symposium on Origin of Matter and Evolution of Galaxies (OMEG15). Journal of the Physical Society of Japan, 2020. http://dx.doi.org/10.7566/jpscp.31.011065.
Byrdwell, William, and Hari Kiran Kotapati. "Adventures in multiple dimensions of chromatography and mass spectrometry for lipidomic analysis." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/athx8798.
Two-dimensional liquid chromatography (2D-LC) is commercially available and has become increasingly common in laboratories across the world. Most 2D-LC systems that are coupled to mass spectrometry use one mass spectrometer attached to the outlet of the second dimension, and the first dimension is reconstructed by “stitching together” the signal from all of the modulation periods. This requires short, fast separations in the second dimension, and fast-scanning mass spectrometers, otherwise “under sampling” can occur. Quantification is problematic using the “blobs” in 2D-LC chromatograms. We have bypassed or eliminated many of the shortcomings or limitations in conventional systems by using multiple mass spectrometers distributed across two or three dimensions of chromatography. We have published results showing the use of split-flow 2D-LC with four mass spectrometers in LC1MS2 × LC1MS2 = LC2MS4 experiments that combined non-aqueous reversed-phase (NARP) HPLC with silver ion chromatography UHPLC for analysis of cis/trans isomers and regioisomers in seed oils, with classic quantification of fat-soluble vitamins (FSVs) and triacylglycerols (TAGs) using direct detection in the first dimension and isomer separation in the second dimension. We have further reported split-flow three-dimensional (3D) LC with four mass spectrometers in LC1MS2 × (LC1MS1 + LC1MS1) = LC3MS4 analysis of infant formula that combined classic quantification of FSVs in the first dimension and TAG quantification by lipidomic analysis in the second dimension. We innovated multi-cycle (a.k.a., “constructive wraparound”) chromatography in the second second dimension for improved separation compared to the conventional approach used in the first second dimension. These and other combinations of LCxMSy are described.
Reports on the topic "Mass spectrometry":
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Benz, Frederick W. High Technology Mass Spectrometry Laboratory. Fort Belvoir, VA: Defense Technical Information Center, August 2010. http://dx.doi.org/10.21236/ada530590.
Hastie, J. W., D. W. Bonnell, and P. K. Schenck. Laser-assisted vaporization mass spectrometry:. Gaithersburg, MD: National Institute of Standards and Technology, 2001. http://dx.doi.org/10.6028/nist.ir.6793.
Hieftje, Gary M., and George H. Vickers. Developments in Plasma-Source Mass Spectrometry. Fort Belvoir, VA: Defense Technical Information Center, July 1988. http://dx.doi.org/10.21236/ada197732.
Gaffney, Amy. Guideline on Isotope Dilution Mass Spectrometry. Office of Scientific and Technical Information (OSTI), May 2017. http://dx.doi.org/10.2172/1358328.
Bach, Stephan B., and Walter Hubert. Radiation Biomarker Research Using Mass Spectrometry. Fort Belvoir, VA: Defense Technical Information Center, July 2007. http://dx.doi.org/10.21236/ada473187.
Perdian, David C. Direct analysis of samples by mass spectrometry: From elements to bio-molecules using laser ablation inductively couple plasma mass spectrometry and laser desorption/ionization mass spectrometry. Office of Scientific and Technical Information (OSTI), January 2009. http://dx.doi.org/10.2172/972075.
Bayne, C. K. Statistical design of mass spectrometry calibration procedures. Office of Scientific and Technical Information (OSTI), November 1996. http://dx.doi.org/10.2172/435300.
Shear, Trevor Allan. Polymer and Additive Mass Spectrometry Literature Review. Office of Scientific and Technical Information (OSTI), June 2017. http://dx.doi.org/10.2172/1363730.
Vertes, Akos. New approaches for metabolomics by mass spectrometry. Office of Scientific and Technical Information (OSTI), July 2017. http://dx.doi.org/10.2172/1368638.
Cook, Kelsey D. Polymer Characterization by Electrohydrodynamic Ionization Mass Spectrometry. Fort Belvoir, VA: Defense Technical Information Center, August 1989. http://dx.doi.org/10.21236/ada212130.
