DOCSLIB.ORG

Thermo Scientific Orbitrap Fusion Tribrid Mass Spectrometer

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
Thermo Scientific 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
  • An Introduction to Isotopic Calculations John M
    An Introduction to Isotopic Calculations John M. Hayes ([email protected]) Woods Hole Oceanographic Institution, Woods Hole, MA 02543, USA, 30 September 2004 Abstract. These notes provide an introduction to: termed isotope effects. As a result of such effects, the • Methods for the expression of isotopic abundances, natural abundances of the stable isotopes of practically • Isotopic mass balances, and all elements involved in low-temperature geochemical • Isotope effects and their consequences in open and (< 200°C) and biological processes are not precisely con- closed systems. stant. Taking carbon as an example, the range of interest is roughly 0.00998 ≤ 13F ≤ 0.01121. Within that range, Notation. Absolute abundances of isotopes are com- differences as small as 0.00001 can provide information monly reported in terms of atom percent. For example, about the source of the carbon and about processes in 13 13 12 13 atom percent C = [ C/( C + C)]100 (1) which the carbon has participated. A closely related term is the fractional abundance The delta notation. Because the interesting isotopic 13 13 fractional abundance of C ≡ F differences between natural samples usually occur at and 13F = 13C/(12C + 13C) (2) beyond the third significant figure of the isotope ratio, it has become conventional to express isotopic abundances These variables deserve attention because they provide using a differential notation. To provide a concrete the only basis for perfectly accurate mass balances. example, it is far easier to say – and to remember – that Isotope ratios are also measures of the absolute abun- the isotope ratios of samples A and B differ by one part dance of isotopes; they are usually arranged so that the per thousand than to say that sample A has 0.3663 %15N more abundant isotope appears in the denominator and sample B has 0.3659 %15N.
    [Show full text]
  • Mass Spectrometry: Quadrupole Mass Filter
    Advanced Lab, Jan. 2008 Mass Spectrometry: Quadrupole Mass Filter The mass spectrometer is essentially an instrument which can be used to measure the mass, or more correctly the mass/charge ratio, of ionized atoms or other electrically charged particles. Mass spectrometers are now used in physics, geology, chemistry, biology and medicine to determine compositions, to measure isotopic ratios, for detecting leaks in vacuum systems, and in homeland security. Mass Spectrometer Designs The first mass spectrographs were invented almost 100 years ago, by A.J. Dempster, F.W. Aston and others, and have therefore been in continuous development over a very long period. However the principle of using electric and magnetic fields to accelerate and establish the trajectories of ions inside the spectrometer according to their mass/charge ratio is common to all the different designs. The following description of Dempster’s original mass spectrograph is a simple illustration of these physical principles: The magnetic sector spectrograph PUMP F DD S S3 1 r S2 Fig. 1: Dempster’s Mass Spectrograph (1918). Atoms/molecules are first ionized by electrons emitted from the hot filament (F) and then accelerated towards the entrance slit (S1). The ions then follow a semicircular trajectory established by the Lorentz force in a uniform magnetic field. The radius of the trajectory, r, is defined by three slits (S1, S2, and S3). Ions with this selected trajectory are then detected by the detector D. How the magnetic sector mass spectrograph works: Equating the Lorentz force with the centripetal force gives: qvB = mv2/r (1) where q is the charge on the ion (usually +e), B the magnetic field, m is the mass of the ion and r the radius of the ion trajectory.
    [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]
  • Good Practice Guide for Isotope Ratio Mass Spectrometry, FIRMS (2011)
    Good Practice Guide for Isotope Ratio Mass Spectrometry Good Practice Guide for Isotope Ratio Mass Spectrometry First Edition 2011 Editors Dr Jim Carter, UK Vicki Barwick, UK Contributors Dr Jim Carter, UK Dr Claire Lock, UK Acknowledgements Prof Wolfram Meier-Augenstein, UK This Guide has been produced by Dr Helen Kemp, UK members of the Steering Group of the Forensic Isotope Ratio Mass Dr Sabine Schneiders, Germany Spectrometry (FIRMS) Network. Dr Libby Stern, USA Acknowledgement of an individual does not indicate their agreement with Dr Gerard van der Peijl, Netherlands this Guide in its entirety. Production of this Guide was funded in part by the UK National Measurement System. This publication should be cited as: First edition 2011 J. F. Carter and V. J. Barwick (Eds), Good practice guide for isotope ratio mass spectrometry, FIRMS (2011). ISBN 978-0-948926-31-0 ISBN 978-0-948926-31-0 Copyright © 2011 Copyright of this document is vested in the members of the FIRMS Network. IRMS Guide 1st Ed. 2011 Preface A few decades ago, mass spectrometry (by which I mean organic MS) was considered a “black art”. Its complex and highly expensive instruments were maintained and operated by a few dedicated technicians and its output understood by only a few academics. Despite, or because, of this the data produced were amongst the “gold standard” of analytical science. In recent years a revolution occurred and MS became an affordable, easy to use and routine technique in many laboratories. Although many (rightly) applaud this popularisation, as a consequence the “black art” has been replaced by a “black box”: SAMPLES GO IN → → RESULTS COME OUT The user often has little comprehension of what goes on “under the hood” and, when “things go wrong”, the inexperienced operator can be unaware of why (or even that) the results that come out do not reflect the sample that goes in.
    [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]
  • 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]
  • Electron Ionization
    Chapter 6 Chapter 6 Electron Ionization I. Introduction ......................................................................................................317 II. Ionization Process............................................................................................317 III. Strategy for Data Interpretation......................................................................321 1. Assumptions 2. The Ionization Process IV. Types of Fragmentation Pathways.................................................................328 1. Sigma-Bond Cleavage 2. Homolytic or Radical-Site-Driven Cleavage 3. Heterolytic or Charge-Site-Driven Cleavage 4. Rearrangements A. Hydrogen-Shift Rearrangements B. Hydride-Shift Rearrangements V. Representative Fragmentations (Spectra) of Classes of Compounds.......... 344 1. Hydrocarbons A. Saturated Hydrocarbons 1) Straight-Chain Hydrocarbons 2) Branched Hydrocarbons 3) Cyclic Hydrocarbons B. Unsaturated C. Aromatic 2. Alkyl Halides 3. Oxygen-Containing Compounds A. Aliphatic Alcohols B. Aliphatic Ethers C. Aromatic Alcohols D. Cyclic Ethers E. Ketones and Aldehydes F. Aliphatic Acids and Esters G. Aromatic Acids and Esters 4. Nitrogen-Containing Compounds A. Aliphatic Amines B. Aromatic Compounds Containing Atoms of Nitrogen C. Heterocyclic Nitrogen-Containing Compounds D. Nitro Compounds E. Concluding Remarks on the Mass Spectra of Nitrogen-Containing Compounds 5. Multiple Heteroatoms or Heteroatoms and a Double Bond 6. Trimethylsilyl Derivative 7. Determining the Location of Double Bonds VI. Library
    [Show full text]
  • Modern Mass Spectrometry
    Modern Mass Spectrometry MacMillan Group Meeting 2005 Sandra Lee Key References: E. Uggerud, S. Petrie, D. K. Bohme, F. Turecek, D. Schröder, H. Schwarz, D. Plattner, T. Wyttenbach, M. T. Bowers, P. B. Armentrout, S. A. Truger, T. Junker, G. Suizdak, Mark Brönstrup. Topics in Current Chemistry: Modern Mass Spectroscopy, pp. 1-302, 225. Springer-Verlag, Berlin, 2003. Current Topics in Organic Chemistry 2003, 15, 1503-1624 1 The Basics of Mass Spectroscopy ! Purpose Mass spectrometers use the difference in mass-to-charge ratio (m/z) of ionized atoms or molecules to separate them. Therefore, mass spectroscopy allows quantitation of atoms or molecules and provides structural information by the identification of distinctive fragmentation patterns. The general operation of a mass spectrometer is: "1. " create gas-phase ions "2. " separate the ions in space or time based on their mass-to-charge ratio "3. " measure the quantity of ions of each mass-to-charge ratio Ionization sources ! Instrumentation Chemical Ionisation (CI) Atmospheric Pressure CI!(APCI) Electron Impact!(EI) Electrospray Ionization!(ESI) SORTING DETECTION IONIZATION OF IONS OF IONS Fast Atom Bombardment (FAB) Field Desorption/Field Ionisation (FD/FI) Matrix Assisted Laser Desorption gaseous mass ion Ionisation!(MALDI) ion source analyzer transducer Thermospray Ionisation (TI) Analyzers quadrupoles vacuum signal Time-of-Flight (TOF) pump processor magnetic sectors 10-5– 10-8 torr Fourier transform and quadrupole ion traps inlet Detectors mass electron multiplier spectrum Faraday cup Ionization Sources: Classical Methods ! Electron Impact Ionization A beam of electrons passes through a gas-phase sample and collides with neutral analyte molcules (M) to produce a positively charged ion or a fragment ion.
    [Show full text]
  • Find the Molar Mass of Sodium Carbonate, Na 2CO3. Na 2 X
    Moles and Molar Mass The mole is the "counting unit" used by chemists to indicate the number of atoms, ions, molecules, or formula units present in a particular chemical sample. The mole is similar to other counting units that you've used before....pair (2), dozen (12), and gross (144). One mole of a compound contains Avogadro's number (6.022 x 1023) of molecules (molecular compound) or formula units (ionic compound). The molar mass of a compound tells you the mass of 1 mole of that substance. In other words, it tells you the number of grams per mole of a compound. The units for molar mass are, therefore, grams/mole. To find the molar mass of a compound: 1. Use the chemical formula to determine the number of each type of atom present in the compound. 2. Multiply the atomic weight (from the periodic table) of each element by the number of atoms of that element present in the compound. 3. Add it all together and put units of grams/mole after the number. Example: Find the molar mass of sodium carbonate, Na2CO3. Na 2 x 23.0 = 46.0 C 1 x 12.0 = 12.0 O 3 x 16.0 = 48.0 molar = 106.0 g/mole mass For many (but not all) problems, you can simply round the atomic weights and the molar mass to the nearest 0.1 g/mole. HOWEVER, make sure that you use at least as many significant figures in your molar mass as the measurement with the fewest significant figures.
    [Show full text]
  • Fundamentals of Biological Mass Spectrometry and Proteomics
    Fundamentals of Biological Mass Spectrometry and Proteomics Steve Carr Broad Institute of MIT and Harvard Modern Mass Spectrometer (MS) Systems Orbitrap Q-Exactive Triple Quadrupole Discovery/Global Experiments Targeted MS MS systems used for proteomics have 4 tasks: • Create ions from analyte molecules • Separate the ions based on charge and mass • Detect ions and determine their mass-to-charge • Select and fragment ions of interest to provide structural information (MS/MS) Electrospray MS: ease of coupling to liquid-based separation methods has made it the key technology in proteomics Possible Sample Inlets Syringe Pump Sample Injection Loop Liquid Autosampler, HPLC Capillary Electrophoresis Expansion of the Ion Formation and Sampling Regions Nitrogen Drying Gas Electrospray Atmosphere Vacuum Needle 3- 5 kV Liquid Nebulizing Gas Droplets Ions Containing Solvated Ions Isotopes Most elements have more than one stable isotope. For example, most carbon atoms have a mass of 12 Da, but in nature, 1.1% of C atoms have an extra neutron, making their mass 13 Da. Why do we care? Mass spectrometers “see” the isotope peaks provided the resolution is high enough. If an MS instrument has resolution high enough to resolve these isotopes, better mass accuracy is achieved. Stable isotopes of most abundant elements of peptides Element Mass Abundance H 1.0078 99.985% 2.0141 0.015 C 12.0000 98.89 13.0034 1.11 N 14.0031 99.64 15.0001 0.36 O 15.9949 99.76 16.9991 0.04 17.9992 0.20 Monoisotopic mass and isotopes We use instruments that resolve the isotopes enabling us to accurately measure the monoisotopic mass MonoisotopicMonoisotopic mass; all 12C, mass no 13C atoms corresponds to 13 lowestOne massC atom peak Two 13C atoms Angiotensin I (MW = 1295.6) (M+H)+ = C62 H90 N17 O14 TheWhen monoisotopic the isotopes mass of aare molecule clearly is the resolved sum of the the accurate monoisotopic masses for the massmost abundant isotope of each element present.
    [Show full text]
  • An Introduction to Mass Spectrometry
    An Introduction to Mass Spectrometry by Scott E. Van Bramer Widener University Department of Chemistry One University Place Chester, PA 19013 [email protected] http://science.widener.edu/~svanbram revised: September 2, 1998 © Copyright 1997 TABLE OF CONTENTS INTRODUCTION ........................................................... 4 SAMPLE INTRODUCTION ....................................................5 Direct Vapor Inlet .......................................................5 Gas Chromatography.....................................................5 Liquid Chromatography...................................................6 Direct Insertion Probe ....................................................6 Direct Ionization of Sample ................................................6 IONIZATION TECHNIQUES...................................................6 Electron Ionization .......................................................7 Chemical Ionization ..................................................... 9 Fast Atom Bombardment and Secondary Ion Mass Spectrometry .................10 Atmospheric Pressure Ionization and Electrospray Ionization ....................11 Matrix Assisted Laser Desorption/Ionization ................................ 13 Other Ionization Methods ................................................13 Self-Test #1 ...........................................................14 MASS ANALYZERS .........................................................14 Quadrupole ............................................................15
    [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]