Even Electron Mass Spectrometry with Biomolecule Applications

The analysis of even electron mass spectra for unknown biomolecule structure identification and elucidation
In addition to providing a practical introduction to mass spectrometry, this bookaddresses the spectral interpretation of even electron mass spectra generated from soft ionization techniques—a fast–growing area with tremendous potentialin biomolecule analysis. From the basics and principles of mass spectrometry to specific applications with examples, Even Electron Mass Spectrometry with Biomolecule Applications covers:
The fundamentals of mass spectrometry, including the approved mass analyzers, reaction rate, and collision theory
Diverse ionization techniques and sources, including electron ionization and the more current soft ionization techniques of electrospray ionization and matrix assisted laser desorption ionization
The basic skills and techniques needed for mass spectral interpretation of even electron ions
Both precursor and product ion mass spectra
Applications to biomolecule analyses, including the analysis of proteins, peptides, DNA/RNA, metabolites, lipids, and carbohydrates
In addition to the essential theoretical background and fundamental principles, this unique reference presents a detailed, step–by–step methodology for interpreting even electron mass spectrometry results. Specific chapters are devoted to: proteomics; biomolecule spectral interpretation of small molecules; biomolecule spectral interpretation of biological macromolecules; and MALDI–TOF–Postsource Decay (PSD). Chapters feature detailed examples, questions, and problems to help readers solidify their understanding of the concepts and techniques.
This is a core reference for scientists and researchers in academic laboratories and pharmaceutical, chemical, and biotech companies. It is also an excellent text for undergraduate or graduate level courses in analytical chemistry, instrumental analysis, biomolecule analysis, and mass spectrometry.

Spis treści:
Preface.
Acknowledgements.
Dedication.
Glossary, Abbreviations, and Definitions.
Chapter I: Introduction and Fundamentals.
1.1 Definition and Description of Mass Spectrometry.
1.2 Basic Design of Mass Analyzer Instrumentation.
1.3 Mass Spectrometry of Protein, Metabolite, and Lipid Biomolecules.
1.3.1 Proteomics.
1.3.2 Metabolomics.
1.3.3 Lipidomics.
1.4 Fundamental Studies of Biological Compound Interactions.
1.5 Mass–to–Charge Ratio (m/z) – How the Mass Spectrometer Separates Ions.
1.6 Exact Mass versus Nominal Mass.
1.7 Mass Accuracy and Resolution.
1.8 High Resolution Mass Measurements.
1.9 Rings Plus Double Bonds (r + db).
1.10 The Nitrogen Rule in Mass Spectrometry.
1.11 Chapter Problems.
1.12 References.
Chapter II: Ionization in Mass Spectrometry.
2.1 Ionization Techniques and Sources.
2.2 Electron Ionization (EI).
2.3 Chemical Ionization (CI).
2.3.1 Positive Chemical Ionization.
2.3.2 Negative Chemical Ionization.
2.4 Atmospheric Pressure Chemical Ionization (APCI).
2.5 Electrospray Ionization (ESI).
2.6 Nano–Electrospray Ionization (nano–ESI).
2.7 Atmospheric Pressure Photo Ionization (APPI).
2.7.1 APPI Mechanism.
2.7.2 APPI VUV Lamps.
2.7.3 APPI Sources.
2.7.4 Comparison of ESI and APPI.
2.8 Matrix Assisted Laser Desorption Ionization (MALDI).
2.9 Fast Atom Bombardment (FAB).
2.9.1 Application of FAB versus EI.
2.10 Chapter Problems.
2.11 References.
Chapter III: Mass Analyzers in Mass Spectrometry.
3.1 Mass Analyzers.
3.2 Magnetic and Electric Sector Mass Analyzer.
3.3 Time–of–Flight Mass Analyzer (TOF/MS).
3.4 Time–of–Flight/Time–of–Flight Mass Analyzer (TOF–TOF/MS).
3.5 Quadrupole Mass Filter.
3.6 Triple Quadrupole Mass Analyzer (QQQ/MS).
3.7 Three Dimensional Quadrupole Ion Trap Mass Analyzer (QIT/MS).
3.8 Linear Quadrupole Ion Trap Mass Analyzer (LTQ/MS).
3.9 Quadrupole/Time–of–Flight Mass Analyzer (Q–TOF/MS).
3.10 Fourier Transform Ion Cyclotron Resonance Mass Analyzer (FTICR/MS).
3.10.1 Introduction.
3.10.2 FTICR Mass Analyzer.
3.10.3 FTICR Trapped Ion Behavior.
3.10.4 Cyclotron and Magnetron Ion Motion.
3.10.5 Basic Experimental Sequence.
3.11 Linear Ion Trap Fourier Transform Mass Analyzer (LTQ–FT/MS).
3.12 Linear Ion Trap Orbitrap Mass Analyzer (LTQ–Orbitrap/MS).
3.13 Chapter Problems.
3.14 References.
Chapter IV: Collision and Unimolecular Reaction Rate Theory.
4.1 Introduction to Collision Theory.
4.2 Non–covalent Bond Dissociation Energy.
4.3 Low Molecular Weight BDE Predictive Model.
4.4 Computer Modeling of BDE Values.
4.5 High Molecular Weight BDE Predictive Model.
4.6 Non–covalent BDE of Li+ Adduct of Mono–pentadecanoin.
4.7 Practice Problems.
4.7.1 Problem 1.
4.7.2 Problem 2.
4.7.3 Problem 3.
4.7.4 Problem 4.
4.7.5 Problem 5.
4.8 BDE Determination of Li+ Lipid Dimer Adducts.
4.9 Covalent Apparent Threshold Energies of Li+ Adducted Acylglycerols.
4.9.1 Apparent Threshold Energy Predictive Model.
4.9.2 Apparent Threshold Energies for Lithiated Mono–pentadecanoin.
4.9.3 Apparent Threshold Energies for Lithiated 1–Stearin,2–palmitin.
4.9.4 Apparent Threshold Energies for Lithiated 1,3–Dipentadecanoin.
4.10 Computational Reaction Enthalpies and Predicted Apparent Threshold Energies.
4.11 Conclusions.
4.12 References.
Chapter V: The Mass Spectrum: Odd Electron Molecular Ion versus Even Electron Precursor Ion Mass Spectra.
5.1 Electron Ionization (EI) Odd Electron (OE) Processes.
5.2 Oleamide Fragmentation Pathways ? Odd Electron M+ú by Gas Chromatography/Electron Io nization–Mass Spectrometry (GC/EI–MS).
5.3 Oleamide Fragmentation Pathways ? Even Electron [M+H]+ by Electrospray Ionization/Ion Trap Mass Spectrometry (ESI/IT–MS).
5.4 Problem: Methyl Oleate EI Mass Spectrum.
5.5 References.
Chapter VI: Product Ion Spectral Interpretation.
6.1 Introduction to Product Ion Spectral Interpretation.
6.2 Structural Elucidation of 1,3–dipentadecanoin.
6.3 Problem: Lithiated Mono–penradecanoin Product Ion Spectrum.
Chapter VII: Proteomics.
7.1 Introduction to Proteomics.
7.2 Protein Structure and Chemistry.
7.3 Bottom–up Proteomics ? Mass Spectrometry of Peptides.
7.3.1 History and Strategy.
7.3.2 Protein Identification Through Product Ion Spectra.
7.3.3 High Energy Product Ions.
7.3.4 De Novo Sequencing.
7.3.5 Electron Capture Dissociation (ECD).
7.4 Top–down Proteomics: Mass Spectrometry of Intact Proteins.
7.4.1 Background.
7.4.2 Gas–Phase Basicity and Protein Charging.
7.4.3 Calculation of Charge State and Molecular Weight.
7.4.4 Top–Down Protein Sequencing.
7.5 Post Translational Modification of Proteins (PTM).
7.5.1 Three Main Types of PTM.
7.5.2 Glycosylation of Proteins.
7.5.3 Phosphorylation of Proteins.
7.5.3.1 Phosphohistidine as Post Translational Modification.
7.5.4 Sulfation of Proteins.
7.5.4.1 Glycosaminoglycan Sulfation.
7.5.4.2 Tyrosine Sulfation.
7.6 Systems Biology and Bioinformatics.
7.6.1 Biomarkers in Cancer.
7.7 Chapter Problems.
7.8 References.
Chapter VIII: Biomolecule Spectral Interpretation – Small Molecules.
8.1 Introduction.
8.2 Ionization Efficiency of Lipids.
8.3 Fatty Acids.
8.3.1 Negative Ion Mode Electrospray Behavior of Fatty Acids.
8.4 Quantitative Analysis by GC/EI Mass Spectrometry.
8.5 Wax Esters.
8.5.1 Oxidized Wax Esters.
8.5.2 Oxidation of Monounsaturated Wax Esters by Fenton Reaction.
8.6