Bibliographies thématiques / Ion mobility separation-mass spectrometry

Littérature scientifique sur le sujet « Ion mobility separation-mass spectrometry »

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Publié le 11 mars 2023

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Articles de revues sur le sujet "Ion mobility separation-mass spectrometry"

R Swetha Sri, B Aishwarya, D Vaishnavi et M Sumakanth. « A review on ion mobility mass spectrometry ». Open Access Research Journal of Biology and Pharmacy 6, n^o 2 (30 novembre 2022) : 013–23. http://dx.doi.org/10.53022/oarjbp.2022.6.2.0067.

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Mass Spectrometry can be coupled with ion mobility to get results that cannot be obtained by alone mass spectrometry. This coupled instrument can be used for knowing the separation of isomers, isobars, and conformers, the reduction of chemical noise, and the measurement of ion size. It divides ions into families of ions as well as ions with the same charge and similar structural properties. The four ion mobility separation techniques currently applied to mass spectrometry are described in this article. Low-resolution mobility separation is demonstrated by AIMS. Offering continuous ion monitorings are DMS and FAIMS. TWIMS is a novel IMS technique that has good sensitivity and is well integrated into a commercial mass spectrometer while having modest resolving power. In this review it includes that Many researches has used this technique has it gives results in millisecond and its low cost operation.it has major drawback of contamination of compounds due to atmospheric pressure, complex spectra and interferences aredue to wide spread of ionization.it is not suitable for Non-volatile compound and the repoducubility is1-2%.

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Garcia, Xavier, Maria Sabaté, Jorge Aubets, Josep Jansat et Sonia Sentellas. « Ion Mobility–Mass Spectrometry for Bioanalysis ». Separations 8, n^o 3 (16 mars 2021) : 33. http://dx.doi.org/10.3390/separations8030033.

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This paper aims to cover the main strategies based on ion mobility spectrometry (IMS) for the analysis of biological samples. The determination of endogenous and exogenous compounds in such samples is important for the understanding of the health status of individuals. For this reason, the development of new approaches that can be complementary to the ones already established (mainly based on liquid chromatography coupled to mass spectrometry) is welcomed. In this regard, ion mobility spectrometry has appeared in the analytical scenario as a powerful technique for the separation and characterization of compounds based on their mobility. IMS has been used in several areas taking advantage of its orthogonality with other analytical separation techniques, such as liquid chromatography, gas chromatography, capillary electrophoresis, or supercritical fluid chromatography. Bioanalysis is not one of the areas where IMS has been more extensively applied. However, over the last years, the interest in using this approach for the analysis of biological samples has clearly increased. This paper introduces the reader to the principles controlling the separation in IMS and reviews recent applications using this technique in the field of bioanalysis.

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Domalain, Virginie, Marie Hubert-Roux, Laurence Quéguiner, Dany JD Fouque, Eric Arnoult, David Speybrouck, Jérôme Guillemont et Carlos Afonso. « Ion mobility-mass spectrometry analysis of diarylquinoline diastereomers : Drugs used for tuberculosis treatment ». European Journal of Mass Spectrometry 25, n^o 3 (5 décembre 2018) : 291–99. http://dx.doi.org/10.1177/1469066718813226.

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Mycobacterium tuberculosis infection results in more than two million deaths per year and is the leading cause of mortality in people infected with HIV. A new structural class of antimycobacterials, the diarylquinolines, has been synthesized and is being highly effective against both M. tuberculosis and multidrug-resistant tuberculosis. As diarylquinolines are biologically active only under their ( R,S) stereoisomeric form, it is essential to differentiate the stereoisomers ( R,S) and ( R,R). To achieve this, tandem mass spectrometry and ion mobility spectrometry-mass spectrometry have been performed with 10 diarylquinoline diastereomers couples. In this study, we investigated cationization with alkali metal cations and several ion mobility drift gases in order to obtain diastereomer differentiations. We have shown that diastereomers of the diarylquinolines family can be differentiated separately by tandem mass spectrometry and in mixture by ion mobility spectrometry-mass spectrometry. However, although the structure of each diastereomer is close, several behaviors could be observed concerning the cationization and the ion mobility spectrometry separation. The ion mobility spectrometry isomer separation efficiency is not easily predictable; it was however observed for all diastereomeric couples with a significant improvement of separation using alkali adducts compared to protonated molecules. With the use of drift gas with higher polarizability only an improvement of separation was obtained in a few cases. Finally, a good correlation of the experimental collision cross section (relative to three-dimensional structure of ions) and the theoretical collision cross section has been shown.

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Pollard, Matthew J., Christopher K. Hilton, Hongli Li, Kimberly Kaplan, Richard A. Yost et Herbert H. Hill. « Ion mobility spectrometer—field asymmetric ion mobility spectrometer-mass spectrometry ». International Journal for Ion Mobility Spectrometry 14, n^o 1 (9 mars 2011) : 15–22. http://dx.doi.org/10.1007/s12127-011-0058-9.

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Ahonen, Linda, Maíra Fasciotti, Gustav Boije af Gennäs, Tapio Kotiaho, Romeu J. Daroda, Marcos Eberlin et Risto Kostiainen. « Separation of steroid isomers by ion mobility mass spectrometry ». Journal of Chromatography A 1310 (octobre 2013) : 133–37. http://dx.doi.org/10.1016/j.chroma.2013.08.056.

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Matz, Laura M., et Herbert H. Hill. « Separation of benzodiazepines by electrospray ionization ion mobility spectrometry–mass spectrometry ». Analytica Chimica Acta 457, n^o 2 (avril 2002) : 235–45. http://dx.doi.org/10.1016/s0003-2670(02)00021-1.

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Lawrence, A. H., et A. A. Nanji. « Ion mobility spectrometry and ion mobility spectrometry/mass spectrometric characterization of dimenhydrinate ». Biological Mass Spectrometry 16, n^o 1-12 (octobre 1988) : 345–47. http://dx.doi.org/10.1002/bms.1200160167.

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Hayashi, Akio, Nobutake Sato, Haruo Hosoda et Ushio Takeda. « Ion Mobility Mass Spectrometry ». Japanese Journal of Pesticide Science 42, n^o 1 (2017) : 187–96. http://dx.doi.org/10.1584/jpestics.w17-55.

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Kanu, Abu B., Prabha Dwivedi, Maggie Tam, Laura Matz et Herbert H. Hill. « Ion mobility-mass spectrometry ». Journal of Mass Spectrometry 43, n^o 1 (16 janvier 2008) : 1–22. http://dx.doi.org/10.1002/jms.1383.

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Ewing, Michael A., Matthew S. Glover et David E. Clemmer. « Hybrid ion mobility and mass spectrometry as a separation tool ». Journal of Chromatography A 1439 (mars 2016) : 3–25. http://dx.doi.org/10.1016/j.chroma.2015.10.080.

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Thèses sur le sujet "Ion mobility separation-mass spectrometry"

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.

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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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Woods, Lucy Ann. « Characterising amyloid assembly using ion mobility spectrometry-mass spectrometry ». Thesis, University of Leeds, 2012. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.590277.

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From small molecules to macromolecules, mass spectrometry has evolved significantly over the past decade, progressing from a tool to identify chemical elements to a powerful technique able to elucidate structural information for large protein complexes. With the interfacing of ion mobility spectrometry to mass spectrometry (IMS-MS), mass spectrometric analyses now occupy an extra dimension, providing unrivalled separation and structural characterisation of lowly-populated species in heterogeneous mixtures. One biological system that has benefitted enormously from such advances is the study of in vitro amyloid formation. The ability of amyloidogenic proteins to assemble into insoluble fibrils is associated with over twenty-five different disease states. Beta-2 microglobulin (β2m) is one such protein able to assemble into amyloid fibrils in vitro, although assembly can only be initiated upon destabilisation of the native structure. Identifying which states initiate fibril formation is challenging. as few techniques are able to separate and characterise such transient species. In addition, recent research has identified a number of small molecule inhibitors of fibrillation and understanding their mechanism of action is a topic of current interest. Here, the power of IMS-MS has been harnessed to achieve the separation and characterisation of monomeric and oligomeric precursors of amyloid fibril formation of the protein β2m. Analysis of oligomeric species populated during fibril formation, in addition to the effects of small molecule inhibitors on oligomer population, has led to the identification of oligomeric species on-pathway to fibril formation. Further investigation into fibrils of different morphologies has also been conducted using IMS and limited proteolysis, Differences in oligomeric populations have been revealed, together with differences in fibril structure. Each of these results highlights how MS can be used to give insights into the mechanism of amyloid formation and highlight the potentials of this approach for screening for potential inhibitors of any assembly reaction.

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Zhou, Li. « Enhanced Electrospray Ionization for Mass Spectrometry and Ion Mobility Spectrometry ». Diss., CLICK HERE for online access, 2006. http://contentdm.lib.byu.edu/ETD/image/etd1384.pdf.

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Ismail, Vian Sdiq Ismail. « Probing lipidation of membrane active peptides and integral membrane proteins by liquid chromatography-mass spectrometry and ion mobility separation-mass spectrometry ». Thesis, Durham University, 2017. http://etheses.dur.ac.uk/12424/.

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Liquid chromatography coupled with mass spectrometry (LC-MS) and tandem mass spectrometry (LC-MS2) are shown to have the sensitivity and functionality to detect protein/peptide modifications by fatty acyl chains in vitro and in vivo studies. Further analysis was also performed by direct infusion ion mobility separation coupled with mass spectrometry (IMS-MS) or tandem mass spectrometry (IMS-MS2). Peptide lipidation in vitro was investigated using the membrane active peptide, melittin. Non-enzymatic melittin lipidation by lysophospholipids has been observed for the first time. When the effect of lysophospholipids was studied in direct competition with diacylphospholipids, the acyl transfer from the lysophospholipids is seen to be preferential with acylation visible after just 3 hour. The longer the interaction time, the greater the amount and number of modifications with double and triple acylation observed after 96 hour. The locations of the modifications identified through LC-MS2 were assigned on different sites of the peptide, including N-terminus, K7, S18, K21, K23, R22 and R24 and with the highest reactivity towards N-terminus and K23. Comparing the lipidation of synthetic melittin (SynM) with the lipidation of naturally occurring melittin from venom of honey bee (BVM) highlights the effect of the PLA2 enzyme that is naturally present in BVM. Here, the action of the enzyme to hydrolyse the diacylphospholipid at the sn-2 position to give the corresponding lysophospholipid is reflected in the acyl transfer to the BVM such that the resulting lysophospholipid clearly dominates the acyl transfer to BVM. In contrast, the acyl transfer to SynM clearly demonstrates that acyl transfer is possible in the absence of an enzyme. In vivo protein lipidation of one of the most abundant integral membrane proteins in mammalian eye lens, AQP0, was also studied. A wide range of acyl groups are shown to modify this protein at the known modification sites, N-terminus and at the amino acid residue K238, many of which are reported here for the first time. These acyl group modifications reflect the biological lipid composition of the membrane leaflet that the acylation sites are proximal to. In an attempt to further distinguish between different forms of lipidated melittin, whether with the same acyl chain modification to different amino acids or to discriminate between palmitoylation and oleoylation modifications, travelling wave ion mobility spectrometry (TWIMS) coupled with MS or MS2 was applied. Results suggested that resolving positional isomers of diacylphospholipids and lysophospholipids (sn-1 vs sn-2 positions) is not possible under the conditions described herein. However, the presence of fatty acyl chains covalently bound to melittin change the conformation of acylated melittin in the gas-phase such that for lower charge states it is possible to suggest a small degree of separation between palmitoylated and oleoylated melittin or their isomers including acylation on N-terminus vs K23. This small degree of separation is enough so that when combined with tandem mass spectrometry, the time-aligned product ion spectra are clearer and improve characterisation. To conclude, the research in this thesis has shown that two of the most abundant biomolecules, lipid and peptides/proteins that are known to exist in close proximity to each other, or interact with each other, are not as chemically inert as previously thought. This reactivity has been reflected herein via aminolysis reaction between membrane lipid composition and each of membrane active peptide, melittin and integral membrane protein, AQP0.

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Ding, Luyi. « Studies of electrospray/ion mobility spectrometry/time-of-flight mass spectrometry ». Thesis, National Library of Canada = Bibliothèque nationale du Canada, 2000. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape2/PQDD_0015/NQ48344.pdf.

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Chawner, Ross. « Combined tandem mass spectrometry and ion mobility spectrometry in proteome analyses ». Thesis, University of Manchester, 2013. https://www.research.manchester.ac.uk/portal/en/theses/combined-tandem-mass-spectrometry-and-ion-mobility-spectrometry-in-proteome-analyses(3ba76f18-4703-4f6e-a97f-ee2b1dfb1deb).html.

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Proteomic studies aim to identify, quantify and characterise the full complement of proteins in a cell or organism under a defined set of conditions, and are important to our understanding of cellular mechanisms. However, such studies represent a major analytical challenge. A typical proteome analysis involves enzyme-mediated digestion of complex protein mixtures to yield an even more complex mixture of peptides. Combined reverse-phase liquid chromatography and tandem mass spectrometry is then traditionally utilised to ascertain sequence information from the characteristic peptide sequences. Analytical data derived for the peptides are employed as search terms in database searching of protein sequences derived from gene sequences. The extreme complexity of the peptide mixtures analysed means that additional novel approaches are required to fully interrogate the vast number of tandem mass spectra generated, assigning peptide identity and thereby helping to address demanding biological questions. The research reported here aims to further our understanding of both gas phase peptide/peptide fragment ion structure and peptide fragmentation behaviour using a combination of tandem mass spectrometry and ion mobility measurement.To facilitate the determination of peptide ion collision cross section, a novel standard, QCAL-IM, produced using the QconCAT strategy, has been developed to enable calibration of drift time in Travelling Wave Ion Mobility instruments. The standard facilitates empirical determination of the rotationally averaged collision cross section of any peptide/peptide fragment ion that lies within the calibration range encompassed. QCAL-IM was subsequently utilised to determine the collision cross section of a range of peptide ions produced by Lys-C and Lys-N proteolysis of ‘standard’ proteins. Data produced allowed the effect upon gas phase ion conformation through changing the location of the basic residue lysine within a peptide sequence to be assessed.The fragmentation behaviour of peptide ions produced by a variety of digestion regimes during both collision-induced dissociation (CID) and electron transfer dissociation (ETD) has also been extensively studied. The proteases trypsin and Lys-C are those typically utilised during proteomic studies and peptides produced by each have either the basic residues arginine or lysine at their carboxy-terminus. Secondary enzymatic treatment with the exoprotease carboxypeptidase B cleaves these basic residues from the C-terminus. Tandem mass spectrometric analysis of both tryptic/Lys-C peptides and their CBPB truncated analogue highlights that the dominant fragment ion series observed during both CID and ETD is determined, at least in part, by the location of such basic residues.Finally, studies were undertaken to investigate the factors which may promote/inhibit scrambling of peptide fragment ion sequence, which has recently been shown to take place during CID. The effect of modifying the gas phase basicity of the N-terminal amino acid residue is studied through a combination of derivatisation and synthesis of alternative peptide sequences. Increasing the gas phase basicity is shown to inhibit the observed sequence scrambling while promoting concomitant rearrangement/retention of a carboxyl oxygen at the C-terminus to give enhanced formation of bn+H2O product ion species.

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Koeniger, Stormy Lee Ann. « Multidimensional ion mobility spectrometry coupled to time-of-flight mass spectrometry ». [Bloomington, Ind.] : Indiana University, 2006. http://gateway.proquest.com/openurl?url_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:dissertation&res_dat=xri:pqdiss&rft_dat=xri:pqdiss:3230539.

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Thesis (Ph. D.)--Indiana University, Dept. of Chemistry, 2006.
Title from PDF t.p. (viewed Nov. 5, 2008). Source: Dissertation Abstracts International, Volume: 67-08, Section: B, page: 4395. Adviser: David E. Clemmer.

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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.

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Smiljanic, Danijela. « Mass Spectrometry Interfaced with Ion Mobility or Liquid Chromatography Separation for the Analysis of Complex Mixtures ». University of Akron / OhioLINK, 2011. http://rave.ohiolink.edu/etdc/view?acc_num=akron1323149449.

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Hofmann, Johanna [Verfasser]. « Ion Mobility-Mass Spectrometry of Complex Carbohydrates / Johanna Hofmann ». Berlin : Freie Universität Berlin, 2017. http://d-nb.info/1141678438/34.

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Livres sur le sujet "Ion mobility separation-mass spectrometry"

Ashcroft, Alison E., et Frank Sobott, dir. Ion Mobility-Mass Spectrometry. Cambridge : Royal Society of Chemistry, 2021. http://dx.doi.org/10.1039/9781839162886.

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Paglia, Giuseppe, et Giuseppe Astarita, dir. Ion Mobility-Mass Spectrometry. New York, NY : Springer US, 2020. http://dx.doi.org/10.1007/978-1-0716-0030-6.

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Shvartsburg, Alexandre A. Differential ion mobility spectrometry : Nonlinear ion transport and fundamentals of FAIMS. Boca Raton : CRC Press, 2008.

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Cross, John H. Third International Workshop on Ion Mobility Spectrometry : Proceedings of an International Speciality Conference co-sponsored by Lyndon B. Johnson Space Center and KRUG Life Sciences, and held at Galveston, Texas, October 16-19, 1994. Sous la direction de Lyndon B. Johnson Space Center et International Workshop on Ion Mobility Spectrometry (3rd : 1994 : Galveston, Texas). Houston, Texas : Lyndon B. Johnson Space Center, 1995.

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Wilkins, Charles L., et Sarah Trimpin. Ion Mobility Spectrometry - Mass Spectrometry. Taylor & Francis Group, 2010.

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Wilkins, Charles L., et Sarah Trimpin. Ion Mobility Spectrometry - Mass Spectrometry : Theory and Applications. Taylor & Francis Group, 2010.

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Wilkins, Charles L., et Sarah Trimpin. Ion Mobility Spectrometry - Mass Spectrometry : Theory and Applications. Taylor & Francis Group, 2010.

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Ion Mobility Spectrometry Mass Spectrometry Theory And Applications. CRC Press, 2010.

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Ion Mobility Spectrometry - Mass Spectrometry : Theory and Applications. Taylor & Francis Group, 2017.

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Ashcroft, Alison E., et Frank Sobott. Ion Mobility-Mass Spectrometry : Fundamentals and Applications. Royal Society of Chemistry, The, 2021.

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Chapitres de livres sur le sujet "Ion mobility separation-mass spectrometry"

Richardson, K., et K. Giles. « CHAPTER 4. Travelling Wave Ion Mobility Separation : Basics and Calibration ». Dans Ion Mobility-Mass Spectrometry, 83–104. Cambridge : Royal Society of Chemistry, 2021. http://dx.doi.org/10.1039/9781839162886-00083.

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McLean, John A., J. Albert Schultz et Amina S. Woods. « Ion Mobility-Mass Spectrometry ». Dans Electrospray and MALDI Mass Spectrometry, 411–39. Hoboken, NJ, USA : John Wiley & Sons, Inc., 2012. http://dx.doi.org/10.1002/9780470588901.ch12.

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Sugai, Toshiki. « Ion Mobility Spectrometry with Mass Spectrometry ». Dans Fundamentals of Mass Spectrometry, 89–107. New York, NY : Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-7233-9_6.

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Stroganova, Iuliia, et Anouk M. Rijs. « CHAPTER 9. Ion Spectroscopy Coupled to Ion Mobility–Mass Spectrometry ». Dans Ion Mobility-Mass Spectrometry, 206–42. Cambridge : Royal Society of Chemistry, 2021. http://dx.doi.org/10.1039/9781839162886-00206.

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Hale, Oliver J., Eva Illes-Toth, Emma K. Sisley et Helen J. Cooper. « CHAPTER 11. Ion Mobility Spectrometry in Mass Spectrometry Imaging ». Dans Ion Mobility-Mass Spectrometry, 272–306. Cambridge : Royal Society of Chemistry, 2021. http://dx.doi.org/10.1039/9781839162886-00272.

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Struwe, W. B. « CHAPTER 18. Glycomics and Ion Mobility ». Dans Ion Mobility-Mass Spectrometry, 496–517. Cambridge : Royal Society of Chemistry, 2021. http://dx.doi.org/10.1039/9781839162886-00496.

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Gabelica, Valérie. « CHAPTER 1. Ion Mobility–Mass Spectrometry : an Overview ». Dans Ion Mobility-Mass Spectrometry, 1–25. Cambridge : Royal Society of Chemistry, 2021. http://dx.doi.org/10.1039/9781839162886-00001.

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Ray, Andrew D., Anthony W. T. Bristow et Stephen W. Holman. « CHAPTER 10. Ion Mobility–Mass Spectrometry of Pharmaceuticals ». Dans Ion Mobility-Mass Spectrometry, 243–71. Cambridge : Royal Society of Chemistry, 2021. http://dx.doi.org/10.1039/9781839162886-00243.

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Ridgeway, M., L. Woods et M. Park. « CHAPTER 5. Trapped Ion Mobility Spectrometry – Basics and Calibration ». Dans Ion Mobility-Mass Spectrometry, 105–31. Cambridge : Royal Society of Chemistry, 2021. http://dx.doi.org/10.1039/9781839162886-00105.

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Fabris, Dan. « CHAPTER 17. Ion Mobility–Mass Spectrometry of Nucleic Acids ». Dans Ion Mobility-Mass Spectrometry, 461–95. Cambridge : Royal Society of Chemistry, 2021. http://dx.doi.org/10.1039/9781839162886-00461.

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Actes de conférences sur le sujet "Ion mobility separation-mass spectrometry"

El-Shafie, Mahmoud Y., Sally Bebawi, Hussein H. Zomor et Frank Gunzer. « Improvement of the ion transfer efficiency in ion mobility spectrometry-mass spectrometry ». Dans 2016 IEEE Workshop on Environmental, Energy, and Structural Monitoring Systems (EESMS). IEEE, 2016. http://dx.doi.org/10.1109/eesms.2016.7504828.

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Isaac, Giorgis, Hernando Olivos et Robert Plumb. « Lipid separation and structural characterization using travelling wave cyclic ion mobility ». Dans 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/snxj7960.

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The analysis and structural characterization of lipids remain challenging due to the chemical structure diversity and isobaric nature. In recent years, liquid chromatography coupled to ion mobility-mass spectrometry (LC-IM-MS) for lipidomics has shown advantages in lipid identification. In particular, collision cross section (CCS) obtained from the IM measurements represents a physical property that can be used to enhance the confidence of lipid identification. Data were collected on a hybrid quadrupole cyclic IM (cIM) orthogonal acceleration time-of-flight instrument. It provides the option to perform either a single pass, or multiple passes until the desired resolution is achieved. MS and CID fragmentation data were obtained on precursor IM separated lipids followed by TOF mass measurement. Using the advanced travelling WAVE technology, a portion of the IMS separation can be selected and stored in a Pre-Array trap region. The stored ions can be re-injected to enable ion mobility analysis and by repeating this IMS to the “n” experiments can be performed. Ion mobility provides additional separation dimension that allows the separation of isobaric and isomeric compounds. The separation and structural characterization of different lipid classes using cIM is currently under study. Different lipid classes with positional isomer (Sn1/Sn2 vs Sn2/Sn1), different double bond positions, cis and trans isomers, glucosyl and galactosyl ceramide isomers, PIP and ganglioside isomers were investigated. Some of the isomers were baseline separated only after 1 pass (approximately at 65 IMS resolution) and others with 50 passes (approximately at 450 IMS resolution). In summary, cyclic IMS provides novel, scalable ion mobility resolution and the increased resolution is useful to resolve and separate isobaric and isomeric lipids species. Advanced modes of operation with ion activation followed by ion mobility separation offers new insights into lipid structural characterization.

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Ekeowa, Ugo I., Joanna Freeke et David Lomas. « The Characterisation Of Alpha1-antitrypsin Polymerisation By Ion Mobility – Mass Spectrometry ». Dans American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a4985.

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Laudien, Robert, Rainer Schultze et Jochen Wieser. « Fast detection of narcotics by single photon ionization mass spectrometry and laser ion mobility spectrometry ». Dans Security + Defence, sous la direction de Colin Lewis, Douglas Burgess, Roberto Zamboni, François Kajzar et Emily M. Heckman. SPIE, 2010. http://dx.doi.org/10.1117/12.864697.

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von Helden, Gert, Gerard Meijer, Jan Horlebein, Eike Mucha et Maike Lettow. « AN ION MOBILITY MASS SPECTROMETRY CRYOGENIC ION TRAP INSTRUMENT COUPLED TO THE FRITZ HABER INSTITUTE INFRARED FREE ELECTRON LASER ». Dans 2021 International Symposium on Molecular Spectroscopy. Urbana, Illinois : University of Illinois at Urbana-Champaign, 2021. http://dx.doi.org/10.15278/isms.2021.rm09.

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Tarver, Edward E. « External second-gate Fourier transform ion mobility spectrometry : parametric optimization for detection of weapons of mass destruction ». Dans Defense and Security, sous la direction de Edward M. Carapezza. SPIE, 2004. http://dx.doi.org/10.1117/12.546800.

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Macht, M., D. E. Damalas, C. Baessmann, N. Borg et N. S. Thomaidis. « Short Lecture “Increasing the confidence in adulteration and authenticity analysis in food by using Trapped Ion Mobility High Resolution Mass Spectrometry” ». Dans GA – 70th Annual Meeting 2022. Georg Thieme Verlag KG, 2022. http://dx.doi.org/10.1055/s-0042-1758936.

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Wei, J., Z. P. Wang, L. Wang, G. Y. Li et Z. Q. Mo. « Low Temperature Anodic Bonding for MEMS Applications ». Dans ASME 2002 International Mechanical Engineering Congress and Exposition. ASMEDC, 2002. http://dx.doi.org/10.1115/imece2002-39272.

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In this paper, anodic bonding between silicon wafer and glass wafer (Pyrex 7740) has been successfully achieved at low temperature. The bonding strength is measured using a tensile testing machine. The interfaces are examined and analyzed by scanning acoustic microscopy (SAM), scanning electron microscopy (SEM) and secondary ion mass spectrometry (SIMS). Prior to bonding, the wafers are cleaned in RCA solutions, and the surfaces become hydrophilic. The effects of the bonding parameters, such as bonding temperature, voltage, bonding time and vacuum condition, on bonding quality are investigated using Taguchi method, and the feasibility of bonding silicon and glass wafers at low temperature is explored. The bonding temperature used ranges from 200 °C to 300 °C. The sensitivity of the bonding parameters is analyzed and it is found that the bonding temperature is the dominant factor for the bonding process. Therefore, the effects of bonding temperature are investigated in detail. High temperatures cause high ion mobility and bonding current density, resulting in the short transition period to the equilibrium state. Almost bubble-free interfaces have been obtained. The bonded area increases with increasing the bonding temperature. The unbonded area is less than 1.5% within the whole wafer for bonding temperature between 200 °C to 300 °C. The bonding strength is higher than 10 MPa, and increases with the bonding temperature. Fracture mainly occurs inside the glass wafer other than in the interface when the bonding temperature is higher than 225 °C. SIMS results show that the chemical bonds of Si-O form in the interface. Higher bonding temperature results in more oxygen migration to the interface and more Si-O bonds. The bonding mechanisms consist of hydrogen bonding and Si-O chemical reaction.

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Chavarría-Miranda, Daniel, Brian Clowers, Gordon Anderson et Mikhail Belov. « Simulating data processing for an advanced ion mobility mass spectrometer ». Dans the 1st international workshop. New York, New York, USA : ACM Press, 2007. http://dx.doi.org/10.1145/1328554.1328563.

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Adamov, Alexey, Heikki Junninen, Jonathan Duplissy, Mikko Sipilä, Markku Kulmala et CLOUD Collaboration. « Cluster measurements at CLOUD using a high resolution ion mobility spectrometer-mass spectrometer combination ». Dans NUCLEATION AND ATMOSPHERIC AEROSOLS : 19th International Conference. AIP, 2013. http://dx.doi.org/10.1063/1.4803275.

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Rapports d'organisations sur le sujet "Ion mobility separation-mass spectrometry"

Bilbao Pena, Aivett. Algorithms and File Structure to Extend and Enhance Liquid Chromatography and Ion Mobility Mass Spectrometry Workflows - CRADA 465. Office of Scientific and Technical Information (OSTI), février 2021. http://dx.doi.org/10.2172/1867247.

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Russell, David H. Developing Ion Mobility-Mass Spectrometry for Structural Characterization of Complex Molecular Systems, Final Report/Product Number : DOE_ER-15520-3. Office of Scientific and Technical Information (OSTI), juin 2017. http://dx.doi.org/10.2172/1430105.

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Bilbao Pena, Aivett. Algorithms and file structures to enhance software workflows for ion mobility mass spectrometry (IM-MS) - CRADA 410 Final Report. Office of Scientific and Technical Information (OSTI), avril 2021. http://dx.doi.org/10.2172/1894883.

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Buratto, Steven K. Final Technical Report for DE-FG02-06ER15835 : Chemical Imaging with 100nm Spatial Resolution : Combining High Resolution Flurosecence Microscopy and Ion Mobility Mass Spectrometry. Office of Scientific and Technical Information (OSTI), septembre 2013. http://dx.doi.org/10.2172/1091803.

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Hunka, Deborah E., et Daniel Austin. Ion Mobility Spectrometer / Mass Spectrometer (IMS-MS). Office of Scientific and Technical Information (OSTI), octobre 2005. http://dx.doi.org/10.2172/1126945.

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Hunka Deborah Elaine et Daniel E. Austin. Ion mobility spectrometer / mass spectrometer (IMS-MS). Office of Scientific and Technical Information (OSTI), juillet 2005. http://dx.doi.org/10.2172/889413.

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Morris, Robert E., Thomas N. Loegel, Kristina M. Myers et Christopher J. Katilie. Analysis of Phenolic Antioxidants in Navy Mobility Fuels by Gas Chromatography-Mass Spectrometry. Fort Belvoir, VA : Defense Technical Information Center, juin 2013. http://dx.doi.org/10.21236/ada587443.

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