DOCSLIB.ORG

Orbitrap Fusion Tribrid Mass Spectrometer

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
Orbitrap Fusion Tribrid Mass Spectrometer MASS SPECTROMETRY Product Specifications Thermo Scientific Orbitrap Fusion Tribrid Mass Spectrometer Unmatched analytical performance, revolutionary MS architecture The Thermo Scientific™ Orbitrap Fusion™ mass spectrometer combines the best of quadrupole, Orbitrap, and linear ion trap mass analysis in a revolutionary Thermo Scientific™ Tribrid™ architecture that delivers unprecedented depth of analysis. It enables life scientists working with even the most challenging samples—samples of low abundance, high complexity, or difficult-to-analyze chemical structure—to identify more compounds faster, quantify them more accurately, and elucidate molecular composition more thoroughly. • Tribrid architecture combines quadrupole, followed by ETD or EThCD for glycopeptide linear ion trap, and Orbitrap mass analyzers characterization or HCD followed by CID • Multiple fragmentation techniques—CID, for small-molecule structural analysis. HCD, and optional ETD and EThCD—are available at any stage of MSn, with The ultrahigh resolution of the Orbitrap mass subsequent mass analysis in either the ion analyzer increases certainty of analytical trap or Orbitrap mass analyzer results, enabling molecular-weight • Parallelization of MS and MSn acquisition determination for intact proteins and confident to maximize the amount of high-quality resolution of isobaric species. The unsurpassed data acquired scan rate and resolution of the system are • Next-generation ion sources and ion especially useful when dealing with complex optics increase system ease of operation and robustness and low-abundance samples in proteomics, • Innovative instrument control software metabolomics, glycomics, lipidomics, and makes setup easier, methods more similar applications. powerful, and operation more intuitive The intuitive user interface of the tune editor The Orbitrap Fusion Tribrid MS can perform and method editor makes instrument calibration a wide variety of analyses, from in-depth and method development easier. The method discovery experiments to characterization of editor also contains a comprehensive library complex PTMs to comprehensive qual/quan of application-specific templates for commonly workflows. The availability of multiple performed analyses. fragmentation techniques—CID, HCD, ETD, and EThCD—at any stage of MSn, with fragment ion detection in either the ion trap or Orbitrap mass analyzer, offers a new level of versatility and performance for the most challenging applications. Users can perform complex MSn experiments such as HCD 2 The optional Thermo Scientific™ EASY-ETD™ Dual-Pressure Linear Ion Trap Performance Characteristics ion source uses Townsend discharge n • High-pressure cell for MS precursor ion Linear Ion Trap Mass Range ionization to generate a highly stable reagent isolation from 0.2 amu to 600 amu Standard – m/z 50–2,000 ion flux. The source is very compact, fitting • Collision-induced dissociation (CID) and High Mass – m/z 200–4,000 inside the mass spectrometer. Intelligent, electron-transfer dissociation (ETD) automated precursor ion sorting routines, Orbitrap Mass Range reagent filtering using the quadrupole mass • Low-pressure cell for improved scan speed, Up to m/z 6000 without precursor ion resolving power, and mass accuracy filter, and charge-state-specific calibration of selection • Dual-dynode detector with high linear ETD reaction time maximize the quality of dynamic range for improved quantitation Resolution ETD spectra. and a large surface area for increased 15,000–500,000 (FWHM) at m/z 200 lifespan and robustness Hardware Specifications Scan Rate (under defined conditions) Vacuum System n Ion Source Orbitrap MS up to 20 Hz • Split-flow turbomolecular pump controlling Ion trap MSn up to 20 Hz Thermo Scientific™ EASY-Max NG™ vacuum in multiple regions Ion Source • Precise and accurate low mTorr pressure Mass Accuracy (under defined conditions) • Outstanding performance without control in the ion-routing multipole <3 ppm RMS using external calibration adjustments • Differentially pumped to ~3 × 10-4 Torr in <1 ppm RMS using internal calibration • Automatic gas and electrical connections the ion trap chamber MS/MS Electrospray Ionization (ESI) on installation -10 • Differentially pumped to <2 × 10 Torr in Ion Trap Sensitivity • Enhanced exhaust port efficiently removes Orbitrap mass analyzer 2 μL of a 50 fg/μL solution of reserpine solvent vapor, improving uptime and (100 fg total) injected at a flow of 500 μL/min reducing chemical noise Options will produce a minimum signal-to-noise ratio ™ ™ Ion Optics Thermo Scientific Ion Max NG Ion Source of 100:1 for the transition of the isolated • Adjustable heated electrospray ionization protonated molecular ions at m/z 609 to S-Lens (HESI) probe for ultimate sensitivity the largest two product ions, m/z 397 and • Progressively spaced stacked-ring ion • Flow rates from 1 μL/min up to m/z 448, when the mass spectrometer is guide (S-Lens) captures and efficiently <2,000 μL/min operated at unit resolution in the full-scan focuses ions in a tight beam MS/MS mode, m/z 165–615. The test • APCI probe compatible with liquid flow requires the HESI probe. • Large variable spacing between electrodes rates of 50 μL/min to 2 mL/min without provides better pumping efficiency and splitting Dynamic Range improved ruggedness ™ ™ >5,000 within a single scan • Automatic tuning program optimizes Thermo Scientific NanoSpray Flex NG transmission Ion Source MS Scan Power • Supports static packed-tip and dynamic MSn, for n = 1 through 10 Active Beam Guide nanoelectrospray experiments • Reduces noise by preventing neutrals and • Compatible with liquid flow rates of Synchronous Precursor Selection high-velocity clusters from entering the 50 nL/min to 2 μL/min Up to 20 precursors per MS2 scan, for MS3 quadrupole mass filter analysis only • Axial field along the length of the rods Thermo Scientific™ EASY-Spray™ Ion Source improves ion transfer robustness • Maximum nanoelectrospray performance Multiplexing Using Ion-Routing Multipole with no need for adjustments Up to 10 precursors per scan using Quadrupole Mass Filter quadrupole mass filter • MS/MS precursor ion selection with high Thermo Scientific™ EASY-ETD™ Ion Source ion transmission from 50 to 3000 m/z • Generates fluoranthene anions for electron Polarity Switching One full cycle in 1.1 sec (one full scan in • Precursor ion isolation window widths from transfer dissociation (ETD) positive mode and one full scan in negative 0.4 amu to 1200 amu • Townsend discharge ionization is extremely mode at resolution setting of 30,000) stable and robust Ion-Routing Multipole • Compact size, located entirely within the ETD Option • Higher-energy collisional dissociation footprint of the instrument ETD fragmentation efficiency of >15% (HCD) cell • Active reagent ion filtering using (infusion of 1 pmol/µL angiotensin at 3 µL/min) • Ion storage with or without fragmentation mass-resolving quadrupole • Efficient and stable ion transfer between Analog Inputs the ion-routing multipole and the Orbitrap Thermo Scientific™ EASY-IC™ Ion Source One (1) analog input (0–1 V), and linear ion trap mass analyzers • Generates internal calibrant ions for One (1) analog (0–10 V) real-time mass calibration on every Orbitrap Mass Analyzer spectrum • Nitrogen-filled C-Trap • Provides <1 ppm RMS mass accuracy • Ultra-high-field Orbitrap mass analyzer with resolving power up to 500,000 FWHM and isotopic fidelity up to 240,000 FWHM at m/z 200 3 Figure 1. Orbitrap Fusion ion path RF-Lens Software Features Data System Exclusive Technologies • High-performance PC with Intel® • Dynamic Scan Management allows for • Data-dependent neutral-loss experiment microprocessor intelligent, real-time scheduling, triggers MS3 scans on only MS/MS • High-resolution LCD color monitor parallelization, and prioritization of the scan product ions with a predefined neutral loss events. It also enables selection, sorting, • Microsoft® Windows® 7 operating system • Isolation window offset allows for custom and routing of precursors to different centering of the isolation window when • Microsoft Office 2010 software fragmentation modes and analyzers based working with broad isotopic distributions ™ ™ on user-selected parameters, including • Thermo Scientific Xcalibur processing • Quanfirmation experiment uses synchronous precursor m/z, intensity, and/or charge. and instrument control software HR/AM SIM for quantitation with full-scan • Tune editor for system calibration, • Precursor fragmentation can take place in MS/MS in the ion trap for precursor diagnostics, and manual data acquisition the ion-routing multipole (HCD), in the ion identity confirmation trap (CID, ETD) or both (EThCD) with • Method editor with comprehensive fragment detection in the linear ion trap or Optional Application-Specific Software application-specific template library and Orbitrap mass analyzers at any stage of ™ ™ drag-and-drop user interface to facilitate • Thermo Scientific Compound Discoverer MSn analysis method development software – integrated solution for • Dynamic exclusion allows acquisition of small-molecule structural identification Operation Modes MS/MS and MSn spectra from lower-intensity • Thermo Scientific™ Mass Frontier™ • Top-speed mode maximizes the number of ion species software – predictive fragmentation high-quality MSn spectra from each cycle • Automatic gain control (AGC) ensures that software for spectral interpretation and by intelligently scheduling MS and the ion trap is always filled with the classification
Load more

Recommended publications
  • Ion Trap Quantum Computer Selected Topics
    Ion Trap Quantum Computer Selected Topics Ruben Andrist & Thomas Uehlinger 1 Outline Ion Traps Part I Deutsch-Josza Deutsch-Josza algorithm Problem Algorithm Implementation Part II Scalability Scalability of ion trap Problem Move ions quantum computers Microtraps Photons Charges Part III Roundup Roundup & Outlook Ruben Andrist Thomas Uehlinger 2 0:98.')4Part+8, 6: ,I39:2 .07.:09 $ " % H " !1 1# %1#% Quantum Algorithms H !1 1# %! 1#% 0"0.9743(.6:-(9 ( 5 ! ! 5 &1 ( 5 " "$1&!' 5 249(43,"6:-(9 # H !1 1# %1#%!4389,39( H !1 1# %! 1#% !,$,3.0/) ":,39:2,3,()8+8 ,+;08 9/0 7+,/9,38107 ,1907 ,8+3,(0 20,8:702039 3 W 0:98.)*# ,48.,*!74. # $4. 343/439*;99> W A0B803*C ):,3E*",3/"C*,2-7A/E0; > Implementation of the Deutsch-Josza Ion Traps algorithm using trapped ions Deutsch-Josza Problem ! show suitability of ion traps Algorithm Implementation ! relatively simple algorithm Scalability Problem ! using only one trapped ion Move ions Microtraps Photons Charges Paper: Nature 421, 48-50 (2 January 2003), doi:10.1038/nature01336; Institut für Experimentalphysik, Universität Innsbruck ! Roundup ! MIT Media Laboratory, Cambridge, Massachusetts Ruben Andrist Thomas Uehlinger 4 The two problems Ion Traps The Deutsch-Josza Problem: Deutsch-Josza ! Bob uses constant or balanced function Problem Alice has to determine which kind Algorithm ! Implementation Scalability Problem The Deutsch Problem: Move ions Bob uses a fair or forged coin Microtraps ! Photons ! Alice has to determine which kind Charges Roundup Ruben Andrist Thomas Uehlinger 5 Four
    [Show full text]
  • Simultaneous Analysis of Drugs in Forensic Cases by Liquid Chromatography–High‑Resolution Orbitrap Mass Spectrometry
    Chromatographia (2020) 83:53–64 https://doi.org/10.1007/s10337-019-03814-w ORIGINAL Simultaneous Analysis of Drugs in Forensic Cases by Liquid Chromatography–High‑Resolution Orbitrap Mass Spectrometry Siti U. Mokhtar1 · Chadin Kulsing2,3,4 · Jalal T. Althakafy2,5 · Alex Kotsos6 · Olaf H. Drummer6,7 · Philip J. Marriott2 Received: 10 May 2019 / Revised: 23 September 2019 / Accepted: 15 October 2019 / Published online: 31 October 2019 © Springer-Verlag GmbH Germany, part of Springer Nature 2019 Abstract In the present study, liquid chromatography coupled to an Orbitrap mass spectrometer (HPLC–Q-Orbitrap MS) was used as an approach for identifcation and quantifcation of 113 drugs simultaneously in biological samples (whole blood/plasma/ serum). Samples were prepared using liquid–liquid extraction conducted using a trizma/isopropanol/butyl chloride bufer system. Reversed-phase separation employing a column (50 × 2.1 mm) packed with 2.6-μm C18 particles was then performed under gradient elution with mobile phase composition consisting of acetic acid and aqueous-acetonitrile mixtures with the acetonitrile content ranging from 10 to 100% v/v. Compounds were detected with high-resolution MS operated in full scan mode having a mass accuracy < 5 ppm. In this study, isobaric compounds (same nominal mass) were easily distinguished and identifed by their diferent retention times. Extracted ion chromatograms (XICs) with narrow mass tolerance window (5 ppm) 2 provided analysis with acceptable linearity (r ) ranged from 0.9530 to 1, low limits of detection (LOD) (0.02–39 ng mL−1) and low limit of quantifcation (LOQ) (0.1–130 ng mL−1). The developed method was applied to successfully analyse drugs in 26 blood samples from positive forensic cases and proved that this technique was able to detect analytes at trace level.
    [Show full text]
  • ADVANCED SPECTROMETER Introduction
    ADVANCED SPECTROMETER Introduction In principle, a spectrometer is the simplest of scientific very sensitive detection and precise measurement, a real instruments. Bend a beam of light with a prism or diffraction spectrometer is a bit more complicated. As shown in Figure grating. If the beam is composed of more than one color of 1, a spectrometer consists of three basic components; a light, a spectrum is formed, since the various colors are collimator, a diffracting element, and a telescope. refracted or diffracted to different angles. Carefully measure The light to be analyzed enters the collimator through a the angle to which each color of light is bent. The result is a narrow slit positioned at the focal point of the collimator spectral "fingerprint," which carries a wealth of information lens. The light leaving the collimator is therefore a thin, about the substance from which the light emanates. parallel beam, which ensures that all the light from the slit In most cases, substances must be hot if they are to emit strikes the diffracting element at the same angle of inci- light. But a spectrometer can also be used to investigate cold dence. This is necessary if a sharp image is to be formed. substances. Pass white light, which contains all the colors of The diffracting element bends the beam of light. If the beam the visible spectrum, through a cool gas. The result is an is composed of many different colors, each color is dif- absorption spectrum. All the colors of the visible spectrum fracted to a different angle. are seen, except for certain colors that are absorbed by the gas.
    [Show full text]
  • Spectrum 100 Series User's Guide
    MOLECULAR SPECTROSCOPY SPECTRUM 100 SERIES User’s Guide 2 . Spectrum 100 Series User’s Guide Release History Part Number Release Publication Date L1050021 A October 2005 Any comments about the documentation for this product should be addressed to: User Assistance PerkinElmer Ltd Chalfont Road Seer Green Beaconsfield Bucks HP9 2FX United Kingdom Or emailed to: [email protected] Notices The information contained in this document is subject to change without notice. Except as specifically set forth in its terms and conditions of sale, PerkinElmer makes no warranty of any kind with regard to this document, including, but not limited to, the implied warranties of merchantability and fitness for a particular purpose. PerkinElmer shall not be liable for errors contained herein for incidental consequential damages in connection with furnishing, performance or use of this material. Copyright Information This document contains proprietary information that is protected by copyright. All rights are reserved. No part of this publication may be reproduced in any form whatsoever or translated into any language without the prior, written permission of PerkinElmer, Inc. Copyright © 2005 PerkinElmer, Inc. Trademarks Registered names, trademarks, etc. used in this document, even when not specifically marked as such, are protected by law. PerkinElmer is a registered trademark of PerkinElmer, Inc. Spectrum, Spectrum 100, and Spectrum 100N are trademarks of PerkinElmer, Inc. Spectrum 100 Series User’s Guide . 3 Contents Contents...............................................................................................
    [Show full text]
  • Mass Spectrometer Business Presentation Materials
    Mass Spectrometer Business Presentation Materials Hiroto Itoi, Corporate Officer Deputy General Manager of the Analytical & Measuring Instruments Division Shimadzu Corporation Jul. 3, 2018 Contents I. Introduction • Expansion of Mass Spectrometry ………………………………………………………………… p.3 • History of Shimadzu's Growth in Mass Spectrometry …………………………………………… p.5 II. Overview of Mass Spectrometers • Operating Principle, Demand Trends, and Vendors ……………………………………………… p.9 • Mass Spectra ………………………………………………………………………………………… p.10 • Configuration of Mass Spectrometers …………………………………………………………… p.11 • Ionization …………………………………………………………………………………………… p.12 • Mass Separation …………………………………………………………………………………… p.14 III. Shimadzu's Mass Spectrometer Business • Product Type ………………………………………………………………………………………… p.17 • Application Software ………………………………………………………………………………… p.18 • Growth Strategy for Mass Spectrometer Business ……………………………………………… p.19 • Expand/Improve Product Lines …………………………………………………………………… p.20 • Measures to Expand Application Fields …………………………………………………………… p.24 • Measures to Automate Data Processing Using AI ……………………………………………… p.25 IV. Summary • Future Direction ……………………………………………………………………………………… p.26 July 2018 Mass Spectrometer Business Presentation Materials 2 I. Introduction Expansion of Mass Spectrometry (1) Why Mass Spectrometry? Mass spectrometry is able to analyze a wide variety of compounds with high accuracy and high efficiency (simultaneous multicomponent analysis). It offers superior characteristics that are especially beneficial in the following fields,
    [Show full text]
  • (ESI) Electrospray Ionization
    Electrospray Ionization (ESI) • sample solution • voltage drop • solvent evaporates is injected between source, away as droplets directly into analyzer generates migrate across gap instrument ionized droplets “sheath gas” Electrospray Ionization (ESI) Injected solution usually includes ionizing agent H+ (from acid), Na+, K+ Large droplets from injected stream Resulting ions can be spontaneously eject singly or multiply smaller droplets (due to charged electrostatic repulsion) Electrospray Ionization (ESI) Multiply charged ions frequently observed. ESI M [M•H]+ + [M•2H]2+ + [M•3H]3+ + ... or [M•Na]+ + [M•2Na]2+ + [M•3Na]3+ + ... multiply lysozyme: charged big > 10 kDa protein (protonated) ions From this series of peaks, how do we determine mass of protein? Charge Ladders in Electrospray Ionization We know two things: 1. Any peak corresponds to [M•nH]n+; ion mass m =M+= M + n, charge z = n. 2. Peak to that peak’s left has one more proton attached, one more charge; ion mass m = M + n + 1, charge z = n + 1. Charge Ladders in Electrospray Ionization Set of simultaneous equations: (observed m/z #1) • z = M + z(H+) (observed m/z #2) • (z + 1) = M + z(H+) + 1 2 1 Charge Ladders in Electrospray Ionization Now performed by computer algorithm Set of simultaneous equations: that searches for ladders, outputs likely mass candidates. 1486 • z = M + z 1372.5 • (z + 1) = M + z + 1 Solution: z = 12 M = 17827.2 [M•13H]13+ 2 [M•12H]1 12+ actual MW lysozyme: 17825.2 If sample contains a mixture of counterions, can get messy. ESI-MS 22-mer single-stranded DNA (difficult to desalt) Atmospheric Pressure Chemical Ionization (APCI) •+ •+ Analogous to CI, but uses discharge to generate N2 /O2 , which then iiionizes evapora tdltllThthiited solvent molecules.
    [Show full text]
  • Advantages of the LTQ Orbitrap for Protein Identification in Complex Digests
    Application Note: 386 Advantages of the LTQ Orbitrap for Protein Identification in Complex Digests Rosa Viner, Terry Zhang, Scott Peterman, and Vlad Zabrouskov, Thermo Fisher Scientific, San Jose, CA, USA Introduction Materials and Methods Key Words Comprehensive, accurate identification of proteins in Sample Preparation • LTQ Orbitrap complex sample mixtures is an important fundamental capability for any proteomics research laboratory. Technology Ten µL of E. coli cell lysate diluted 20-fold with 6 M • Peptide advancements in both hardware and software continue to guanidine HCl in 50 mM ammonium bicarbonate (pH 8.0) Sequencing expand and refine our view of any proteomic system in was reduced with 5 mM DTT, alkylated with 25 mM iodoacetic acid and digested at 37 °C for 16 hours. • Protein terms of protein identities and their post-translational Identification modifications (PTMs). It has been suggested that the very HPLC recent ability to routinely obtain accurate mass measurements Column: C18 Packed tip, 75 µm x 75 mm (QSTAR Elite); • PTMs (< 5 ppm RMS) on precursor and MS/MS fragment ions C18 column, 75 µm x 100 mm (LTQ Orbitrap XL) in proteomic experiments should lead to unprecedented Mobile phase A: 0.1% Formic Acid in Water with accuracy in the ability to identify and characterize proteins.1 2% Acetonitrile This paper compares alternative approaches to this Mobile phase B: 0.1% Formic Acid in Acetonitrile challenging application using two high performance Flow Rate: 300 nL/min platforms for proteomics: a QqTOF instrument (QSTAR® Gradient: 5% B to 35% B in 90 min Elite from Applied Biosystems) and a hybrid linear ion trap- orbitrap instrument (Thermo Scientific LTQ Orbitrap XL).
    [Show full text]
  • Experiment 2 Radiation in the Visible Spectrum Emission Spectra Can Be
    Experiment 2 Radiation in the Visible Spectrum Emission spectra can be a unique fingerprint of an atom or molecule. The photon energies and wavelengths are directly related to the allowed quantum energy states of the system. In the following experiments we will examine the radiation given off by sources radiating in the visible region. We will be using a spectrometer produced by Ocean Optics. Light enters the spectrometer via a fiber optic cable. Inside the spectrometer a diffraction grating diffracts the different frequencies onto a CCD. The CCD basically ”counts” the photons according to wavelength. The data is transferred via a usb port to a PC. The Ocean Optics software displays the spectrum as counts versus wavelength. We will examine the spectra given off by the following sources: incandescent light filament, hydrogen, helium, various light emitting diodes and a laser pointer. You will also be given an unknown gas discharge tube and will need to identify the gas via its spectral emissions Pre Lab 1) Obtain a spectrum for hydrogen, mercury, sodium and neon gas emissions. The spectrum must contain an accurate listing of major emission lines (in nm), not simply a color photo of the emission. 2) Make yourself familiar with the manual for the spectrometer and the software. These are available via the following links: http://www.oceanoptics.com/technical/hr4000.pdf http://www.oceanoptics.com/technical/SpectraSuite.pdf These documents are also available on Black Board. 3) How does the Ocean Optics spectrometer work? In your answer list its three main components and describe what each component does.
    [Show full text]
  • 240 Ion Trap GC/MS External Ionization User's Guide
    Agilent 240 Ion Trap GC/MS External Ionization User’s Guide Agilent Technologies Notices © Agilent Technologies, Inc. 2011 Warranty (June 1987) or DFAR 252.227-7015 (b)(2) (November 1995), as applicable in any No part of this manual may be reproduced The material contained in this docu- technical data. in any form or by any means (including ment is provided “as is,” and is sub- electronic storage and retrieval or transla- ject to being changed, without notice, tion into a foreign language) without prior Safety Notices agreement and written consent from in future editions. Further, to the max- Agilent Technologies, Inc. as governed by imum extent permitted by applicable United States and international copyright law, Agilent disclaims all warranties, CAUTION either express or implied, with regard laws. to this manual and any information A CAUTION notice denotes a Manual Part Number contained herein, including but not hazard. It calls attention to an oper- limited to the implied warranties of ating procedure, practice, or the G3931-90003 merchantability and fitness for a par- like that, if not correctly performed ticular purpose. Agilent shall not be or adhered to, could result in Edition liable for errors or for incidental or damage to the product or loss of First edition, May 2011 consequential damages in connection important data. Do not proceed with the furnishing, use, or perfor- beyond a CAUTION notice until the Printed in USA mance of this document or of any indicated conditions are fully Agilent Technologies, Inc. information contained herein. Should understood and met. 5301 Stevens Creek Boulevard Agilent and the user have a separate Santa Clara, CA 95051 USA written agreement with warranty terms covering the material in this document that conflict with these WARNING terms, the warranty terms in the sep- A WARNING notice denotes a arate agreement shall control.
    [Show full text]
  • Contents • Introduction to Proteomics and Mass Spectrometry
    Contents • Introduction to Proteomics and Mass spectrometry - What we need to know in our quest to explain life - Fundamental things you need to know about mass spectrometry • Interfaces and ion sources - Electrospray ionization (ESI) - conventional and nanospray - Heated nebulizer atmospheric pressure chemical ionization - Matrix assisted laser desorption • Types of MS analyzers - Magnetic sector - Quadrupole - Time-of-flight - Hybrid - Ion trap In the next step in our quest to explain what is life The human genome project has largely been completed and many other genomes are surrendering to the gene sequencers. However, all this knowledge does not give us the information that is needed to explain how living cells work. To do that, we need to study proteins. In 2002, mass spectrometry has developed to the point where it has the capacity to obtain the "exact" molecular weight of many macromolecules. At the present time, this includes proteins up to 150,000 Da. Proteins of higher molecular weights (up to 500,000 Da) can also be studied by mass spectrometry, but with less accuracy. The paradigm for sequencing of peptides and identification of proteins has changed – because of the availability of the human genome database, peptides can be identified merely by their masses or by partial sequence information, often in minutes, not hours. This new capacity is shifting the emphasis of biomedical research back to the functional aspects of cell biochemistry, the expression of particular sets of genes and their gene products, the proteins of the cell. These are the new goals of the biological scientist: o to know which proteins are expressed in each cell, preferably one cell at a time o to know how these proteins are modified, information that cannot necessarily be deduced from the nucleotide sequence of individual genes.
    [Show full text]
  • An Organic Chemist's Guide to Electrospray Mass Spectrometric
    molecules Review An Organic Chemist’s Guide to Electrospray Mass Spectrometric Structure Elucidation Arnold Steckel 1 and Gitta Schlosser 2,* 1 Hevesy György PhD School of Chemistry, ELTE Eötvös Loránd University, Pázmány Péter sétány 1/A, 1117 Budapest, Hungary; [email protected] 2 Department of Analytical Chemistry, ELTE Eötvös Loránd University, Pázmány Péter sétány 1/A, 1117 Budapest, Hungary * Correspondence: [email protected] Received: 16 January 2019; Accepted: 8 February 2019; Published: 10 February 2019 Abstract: Tandem mass spectrometry is an important tool for structure elucidation of natural and synthetic organic products. Fragmentation of odd electron ions (OE+) generated by electron ionization (EI) was extensively studied in the last few decades, however there are only a few systematic reviews available concerning the fragmentation of even-electron ions (EE+/EE−) produced by the currently most common ionization techniques, electrospray ionization (ESI) and atmospheric pressure chemical ionization (APCI). This review summarizes the most important features of tandem mass spectra generated by collision-induced dissociation fragmentation and presents didactic examples for the unexperienced users. Keywords: tandem mass spectrometry; MS/MS fragmentation; collision-induced dissociation; CID; ESI; structure elucidation 1. Introduction Electron ionization (EI), a hard ionization technique, is the method of choice for analyses of small (<1000 Da), nonpolar, volatile compounds. As its name implies, the technique involves ionization by electrons with ~70 eV energy. This energy is high enough to yield very reproducible mass spectra with a large number of fragments. However, these spectra frequently lack the radical type molecular ions (M+) due to the high internal energy transferred to the precursors [1].
    [Show full text]
  • Methods of Ion Generation
    Chem. Rev. 2001, 101, 361−375 361 Methods of Ion Generation Marvin L. Vestal PE Biosystems, Framingham, Massachusetts 01701 Received May 24, 2000 Contents I. Introduction 361 II. Atomic Ions 362 A. Thermal Ionization 362 B. Spark Source 362 C. Plasma Sources 362 D. Glow Discharge 362 E. Inductively Coupled Plasma (ICP) 363 III. Molecular Ions from Volatile Samples. 364 A. Electron Ionization (EI) 364 B. Chemical Ionization (CI) 365 C. Photoionization (PI) 367 D. Field Ionization (FI) 367 IV. Molecular Ions from Nonvolatile Samples 367 Marvin L. Vestal received his B.S. and M.S. degrees, 1958 and 1960, A. Spray Techniques 367 respectively, in Engineering Sciences from Purdue Univesity, Layfayette, IN. In 1975 he received his Ph.D. degree in Chemical Physics from the B. Electrospray 367 University of Utah, Salt Lake City. From 1958 to 1960 he was a Scientist C. Desorption from Surfaces 369 at Johnston Laboratories, Inc., in Layfayette, IN. From 1960 to 1967 he D. High-Energy Particle Impact 369 became Senior Scientist at Johnston Laboratories, Inc., in Baltimore, MD. E. Low-Energy Particle Impact 370 From 1960 to 1962 he was a Graduate Student in the Department of Physics at John Hopkins University. From 1967 to 1970 he was Vice F. Low-Energy Impact with Liquid Surfaces 371 President at Scientific Research Instruments, Corp. in Baltimore, MD. From G. Flow FAB 371 1970 to 1975 he was a Graduate Student and Research Instructor at the H. Laser Ionization−MALDI 371 University of Utah, Salt Lake City. From 1976 to 1981 he became I.
    [Show full text]