Mass Spectrometry

Name: Mass Spectrometry | An Applied Approach
Brand: Wiley-Scrivener
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An Applied Approach

Marek Smoluch Giuseppe Grasso Piotr Suder Jerzy Silberring(Herausgeber*in)

Wiley-Scrivener (Verlag)

2. Auflage

Erschienen am 17. Juni 2019

448 Seiten

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Beschreibung

Provides a comprehensive description of mass spectrometry basics, applications, and perspectives

Mass spectrometry is a modern analytical technique, allowing for fast and ultrasensitive detection and identification of chemical species. It can serve for analysis of narcotics, counterfeit medicines, components of explosives, but also in clinical chemistry, forensic research and anti-doping analysis, for identification of clinically relevant molecules as biomarkers of various diseases. This book describes everything readers need to know about mass spectrometry--from the instrumentation to the theory and applications. It looks at all aspects of mass spectrometry, including inorganic, organic, forensic, and biological MS (paying special attention to various methodologies and data interpretation). It also contains a list of key terms for easier and faster understanding of the material by newcomers to the subject and test questions to assist lecturers.

Knowing how crucial it is for young researchers to fully understand both the power of mass spectrometry and the importance of other complementary methodologies, Mass Spectrometry: An Applied Approach teaches that it should be used in conjunction with other techniques such as NMR, pharmacological tests, structural identification, molecular biology, in order to reveal the true function(s) of the identified molecule.

* Provides a description of mass spectrometry basics, applications and perspectives of the technique

* Oriented to a broad audience with limited or basic knowledge in mass spectrometry instrumentation, theory, and its applications in order to enhance their competence in this field

* Covers all aspects of mass spectrometry, including inorganic, organic, forensic, and biological MS with special attention to application of various methodologies and data interpretation

* Includes a list of key terms, and test questions, for easier and faster understanding of the material

Mass Spectrometry: An Applied Approach is highly recommended for advanced students, young scientists, and anyone involved in a field that utilizes the technique.

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Inhalt

Intro
Title Page
Copyright Page
Contents
List of Contributors
Preface
Chapter 1 Introduction
Chapter 2 A Brief History of Mass Spectrometry
Chapter 3 Basic Definitions
Chapter 4 Instrumentation
4.1 Ionization Methods
4.1.1 Electron Ioniza tion (EI)
4.1.2 Chemical Ionizatio n (CI)
4.1.2.1 Principle of Operation: Positive and Negative Ion Modes
4.1.3 Atmospheric Pressure Ionization (API)
4.1.3.1 Atmospheric Pressure Chemical Ionization (APCI)
4.1.3.2 Electrospray Ionization (ESI)
4.1.3.3 Nanoelectrospray
4.1.3.4 Desorption Electrospray Ionization (DESI)
4.1.3.5 Laser Ablation Electrospray Ionization (LAESI)
4.1.3.6 Photoionization
4.1.4 Ambient Plasma-Based Ionization Techniques
4.1.4.1 Introduction
4.1.4.2 Direct Analysis in Real Time (DART)
4.1.4.3 Flowing Atmospheric Pressure Afterglow (FAPA)
4.1.4.4 Dielectric Barrier Discharge Ionization (DBDI)
4.1.5 Matrix-Assisted Laser Desorption/Ionization (MALDI)
4.1.5.1 Introduction
4.1.5.2 The Role of Matrix
4.1.5.3 Atmospheric Pressure MALDI
4.1.5.4 MALDI Mass Spectra Interpretation
4.1.5.5 Desorption/Ionization on Porous Silicon (DIOS)
4.1.5.6 Surface-Enhanced Laser Desorption/Ionization (SELDI)
4.1.5.7 Nanostructure-Enhanced Laser Desorption/Ionization (NALDI)
4.1.5.8 Summary
4.1.6 Inductively Coupled Plasma Ionization (ICP)
4.1.6.1 Introduction
4.1.6.2 ICP as a Technique of Elemental Analysis and ICP Principle
4.1.6.3 Ionization of Elements and Ionization Efficiency
4.1.6.4 Mechanism of ICP Formation
4.1.6.5 Ways of Plasma View and Plasma Generation
4.1.6.6 Sample Introduction
4.1.6.7 Measurement in the ICP-MS Technique
4.1.6.8 Analyzers in ICP-MS Spectrometers
4.1.7 Secondary Ion Mass Spectrometry with Time-of-FlightAnalyzer (TOF-SIMS)
4.1.7.1 Introduction
4.1.7.2 TOF-SIMS Principle of Operation
4.1.7.3 The Sputtering of the Sample Surface
4.1.7.4 Ionization (Generating Secondary Ions)
4.1.7.5 Construction of TOF-SIMS
4.1.7.6 Analytical Capabilities of TOF-SIMS
4.1.7.7 Examples and Spectra Interpretation
4.2 Analyzers
4.2.1 Time of Flight (TOF)
4.2.1.1 Introduction
4.2.1.2 The Working Rule of TOF Analyzer
4.2.1.3 Linear Mode of Operation of TOF
4.2.1.4 The Spread of the Kinetic Energy Regarding the Ions of the Same Mass
4.2.1.5 Delayed Ion Extraction
4.2.1.6 The Reflection Mode
4.2.1.7 Orthogonal Acceleration TOF Analyzer
4.2.1.8 Summary
4.2.2 Ion Mobility Analyzer (IM)
4.2.2.1 Principle of IM Operation
4.2.2.2 Drift Time IMS
4.2.2.3 High Field Asymmetric Waveform Ion Mobility Spectrometer (FAIMS)
4.2.2.4 Traveling Wave Ion Guides (TWIG)
4.2.2.5 IM Spectrum
4.2.2.6 Applications
4.2.3 Quadrupole Mass Analyzer
4.2.3.1 Construction and Principles of Operation of a Quadrupole
4.2.3.2 Behavior of an Ion Inside the Quadrupole
4.2.3.3 How Mass Spectrum Is Generated? Changes of U and V
4.2.3.4 Spectrum Quality
4.2.3.5 Applications of the Quadrupole Analyzer
4.2.3.6 Quadrupoles, Hexapoles, and Octapoles as Focusing Elements: Ion Guides
4.2.4 Ion Trap (IT)
4.2.4.1 Introduction
4.2.4.2 Behavior of an Ion Inside the Ion Trap
4.2.4.3 Analysis of the Ions
4.2.4.4 Mass Selective Instability Mode
4.2.4.5 Resonant Ejection Mode
4.2.4.6 Axial Modulation
4.2.4.7 Nonlinear Resonance
4.2.4.8 Linear Ion Trap (LIT)
4.2.4.9 Applications
4.2.5 High-Resolution Mass Spectrometry
4.2.5.1 Introduction
4.2.6 Ion Cyclotron Resonance (ICR)
4.2.6.1 Introduction
4.2.6.2 Cyclotron Frequency
4.2.6.3 ICR: Principles of Operation
4.2.6.4 Injection of Ions into the ICR Cell
4.2.6.5 Trapping Electrodes
4.2.6.6 Excitation Electrodes
4.2.6.7 Detection Electrodes and Fourier Transform
4.2.6.8 FT-ICR Properties as m/z Analyzer
4.2.7 Orbitrap
4.2.7.1 History of Development and Principles of Operation
4.2.7.2 Analyzing Ions in the Orbitrap
4.2.7.3 Orbitrap Properties as m/z Analyzer
4.2.7.4 Analytical and Proteomic Applications of Orbitrap
4.2.8 Hybrid Mass Spectrometers
4.2.8.1 A Brief Comparison of Mass Analyzers
4.2.8.2 Triple Quadrupoles
4.2.8.3 Q-IT
4.2.8.4 Q-Orbitrap
4.2.8.5 Q-TOF
4.2.8.6 IT-TOF
4.2.8.7 IT-Orbitrap
4.2.9 Sector Instruments
4.2.9.1 Introduction
4.2.9.2 Rule of Operation of Magnetic Analyzer (B)
4.2.9.3 Electrostatic Sector (E)
4.2.9.4 Mass Spectrometers with Magnetic and Electrostatic Sector
4.3 Ion Detectors
4.3.1 Introduction
4.3.2 Electron Multiplier
4.3.3 Microchannel Detector
4.3.4 Medipix/Timepix Detector
4.3.5 Ion Detection in ICR and Orbitrap-Based Mass Spectrometers
Chapter 5 Hyphenated Techniques
5.1 Gas Chromatography Combined with Mass Spectrometry (GC-MS)
5.1.1 Introduction
5.1.2 Detectors
5.1.3 Chemical Modifications: Derivatization
5.1.4 GC-MS Analysis
5.1.5 Two-Dimensional Gas Chromatography Linked to Mass Spectrometry 2D GC-MS
5.2 Liquid Chromatography Linked to Mass Spectrometry (LC-MS)
5.2.1 Introduction
5.2.2 Introduction to Liquid Chroma tography
5.2.3 Types of Detecto rs
5.2.4 Chromatographic Col umns
5.2.5 Chromatographic Separation an d Quantitation Using MS as a Detector
5.2.6 Construction of an Interface Linking Liquid Chromatograph to the Mass Spe ctrometer
5.2.6.1 Introduction
5.2.6.2 ESI Interface
5.2.6.3 APCI Connection to MS
5.2.6.4 APPI Interface
5.2.6.5 LC Connection to MALDI-MS
5.2.6.6 Multidimensional Separations
5.3 Capillary Electrophoresis Linked to Mass Spectrometry
5.3.1 Introduction
5.3.2 Types of Electrophoretic Techniques
5.3.3 Capillary Electrophoresis Linked to ESI
5.3.3.1 Introduction
5.3.3.2 Liquid Sheath Connection
5.3.3.3 Sheath-Free Connection
5.3.3.4 Liquid Junction
5.3.4 Capillary Electrophoresis Linked to Matrix-Assisted Laser Desorption/Ionization
5.3.4.1 Offline CE-MALDI-TOF
5.3.4.2 Direct CE-MALDI-TOF
5.3.4.3 Online CE-MALDI-TOF
5.3.5 Summary
Chapter 6 Mass Spectrometry Imaging
6.1 Introduction
6.2 SIMS
6.3 MALDI-IMS
6.4 DESI
6.5 Analysis of Tissue Sections Using MSI Techniques
6.6 Analysis of Individual Cells and Cell Cultures Using MSI Techniques
6.7 Analysis with MSI Techniques: Examples
6.8 Combinations of Different Imaging Techniques
6.9 Summary
Chapter 7 Tandem Mass Spectrometry
7.1 Introduction
7.2 Principles
7.3 Strategies for MS/MS Experiments
7.3.1 Tandem in Space
7.3.2 Tandem in Time
7.3.3 Multiple Fragmentation
7.4 Fragmentation Techniques
7.4.1 Introduction
7.4.2 (Low-Energy) Collision-Induced Dissociation (CID)
7.4.3 High-Energy Collisional Dissociation (HCD)
7.4.4 Pulsed Q Collision-Induced Dissociation (PQD)
7.4.5 Electron Capture Dissociation (ECD)
7.4.6 Electron Transfer Dissociation (ETD)
7.4.7 Electron Detachment Dissociation (EDD)
7.4.8 Negative Electron Transfer Dissociation (NETD)
7.4.9 Infrared Multiphoton Dissociation (IRMPD)
7.4.10 Blackbody Infrared Radiative Dissociation (BIRD)
7.4.11 Post-source Decay (PSD): Metastable Ion Dissociation
7.4.12 Surface-Induced Dissociation (SID)
7.4.13 Charge Remote Fragmentation
7.4.14 Chemically Activated Fragmentation (CAF)
7.4.15 Proton Transfer Reaction (PTR)
7.5 Practical Aspects of Fragmentation in Mass Spectrometers
7.5.1 In-Source Fragmentation
7.5.2 Triple Quadrupole Fragmentation
7.5.3 Ion Traps
7.5.4 Time-of-Flight Analyzers
7.5.5 Combined Time-of-Flight Analyzers (TOF/TOF)
7.5.6 Hybrid Instruments
7.5.7 Mass Spectrometers Equipped with Orbitrap Analyzer
7.6 Applications of Tandem Mass Spectrometry in Life Sciences
7.7 SWATH Fragmentation
Chapter 8 Mass Spectrometry Applications
8.1 Mass Spectrometry in Proteomics
8.1.1 Introduction
8.1.2 Bottom-Up Versus Top-Down Proteomics
8.1.2.1 Bottom-Up Proteomics
8.1.2.2 Top-Down Proteomics
8.1.3 Database Search and Protein Identification
8.1.4 In-Depth Structural Characterization of a Single Protein: An Example
8.1.5 Quantitative Analysis in Proteomics
8.1.5.1 Introduction
8.1.5.2 Isobaric Tags for Relative and Absolute Quantitation (iTRAQ)
8.1.5.3 Isotope-Coded Affinity Tagging (ICAT)
8.1.5.4 Stable Isotope Labeling in Culture (SILAC)
8.1.5.5 Stable Isotope Labeling of Mammals (SILAM)
8.1.5.6 Mass-Coded Abundance Tagging (MCAT)
8.1.5.7 Label-Free Techniques
8.2 Food Proteomics
8.3 Challenges in Analysis of Omics Data Generated by Mass Spectrometry
8.3.1 Introduction
8.3.1.1 How Big Must Big Data Be?
8.3.1.2 Do Omics Experiments Generate Unstructured Data?
8.3.2 Targeted and Full Unbiased Omics Analysis Based on MS Technology
8.3.2.1 Factors Affecting Data Quality
8.3.2.2 Speed of MS Data Acquisition: Why Does It Matter?
8.3.2.3 Analytical Strategies in Omics Studies
8.3.3 Data Analysis and Visualization of Mass Spectrometry Omics Data
8.3.3.1 A Brief Introduction to Data Visualization
8.3.3.2 Exploration and Preparation of Data for Downstream Statistics and Visualization
8.3.3.3 Differential Expression Analysis
8.3.3.4 Strategies for Visualization Beyond Three Dimensions
8.3.3.5 Bioinformatics Tools
8.3.4 Databases and Search Algorithms
8.3.4.1 Databases for Proteomics
8.3.5 Validation of High-Throughput Data: Current Challenges
8.3.5.1 Analytical Validation
8.3.5.2 Statistical Validation
8.3.5.3 Bioinformatics Validation
8.3.6 Summary and Conclusions
8.4 Application of the Mass Spectrometric Techniques in the Earth Sciences
8.4.1 Introduction
8.4.2 Conventional Geochronology
8.4.3 In Situ Geochronology
8.4.4 Geochemical and Isotopic Tracing
8.5 Mass Spectrometry in Space
8.5.1 Solar Wind and Plasma
8.5.2 Atmospheres of Planets and Moons
8.5.3 Comets
8.5.4 Interstellar and Cometary Dust
8.6 Mass Spectrometry in the Study of Art and Archaeological Objects
8.6.1 Introduction
8.6.2 MS Methods for the Study of Inorganic Components of Art and Archaeological Objects
8.6.3 MS Methods for the Study of Organic Components of Art and Archaeological Objects
8.7 Application of ICP-MS for Trace Elemental and Speciation Analysis
8.7.1 Introduction
8.7.2 Speciation Analysis by ICP-MS: Examples of Applications
8.7.3 Single-Particle and Single-Cell Analysis by ICP-MS: Examples of Applications
8.7.4 Imaging by LA-ICP-MS Technique
8.7.5 Improvements of LA-ICP-MS Technique
8.7.6 LA-ICP Mass Spectrometer with LIBS
8.8 Mass Spectrometry in Forensic Research
8.8.1 Introduction
8.8.2 Forgery in Art
8.8.3 Psychoactive Substances and Narcotics
8.8.4 Counterfeit Drugs and Generation of Metabolites
8.8.5 Terrorism/Explosives/Chemical Warfare
8.8.6 Future Prospects
8.9 Doping in Sport
8.10 Miniaturization in Mass Spectrometry
Chapter 9 Appendix
9.1 Pressure Units
9.2 Most Commonly Detected Fragments Generated by Electron Impact (EI) Ionization
9.3 Trypsin Autolysis Products
9.4 Proteolytic Enzymes for Protein Identification
9.5 Molecular Masses of Amino Acid Residues
9.6 Molecular Masses of Less Common Amino Acid Residues
9.7 Internet Databases
9.7.1 Literature Databases
9.7.2 Scientific Journals
9.7.2.1 Journals Related to Mass Spectrometry
9.7.3 Bioinformatics Databases
9.7.3.1 Protein Databases
9.7.3.2 Database of Structures and Functions of Protein
9.7.3.3 Other Databases
9.7.4 Bioinformatics Tools
9.7.5 Useful Websites
Chapter 10 Abbreviations
Index
EULA

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