Time-Resolved Mass Spectrometry E-Book

Pawel L. Urban

• Herausgeber: John Wiley & Sons
• Kategorie: Wissenschaft und neue Technologien
• Sprache: Englisch

Seitenzahl: 752

Veröffentlichungsjahr: 2016

Beschreibung

Time is an important factor in physical and natural sciences. It characterizes the progress of chemical and biochemical processes. Mass spectrometry provides the means to study molecular structures by detecting gas-phase ions with the unique mass-to-charge ratios. Time-resolved mass spectrometry (TRMS) allows one to differentiate between chemical states that can be observed sequentially at different time points. Real-time mass spectrometric monitoring enables recording data continuously with a specified temporal resolution. The TRMS approaches – introduced during the past few decades – have shown temporal resolutions ranging from hours down to microseconds and beyond.
This text covers the key aspects of TRMS. It introduces ion sources, mass analyzers, and interfaces utilized in time-resolved measurements; discusses the influence of data acquisition and treatment; finally, it reviews most prominent applications of TRMS – in the studies of reaction kinetics and mechanism, physicochemical phenomena, protein structure dynamics, biocatalysis, and metabolic profiling.
It will assist science and engineering students to gain a basic understanding of the TRMS concept, and to recognize its usefulness. In addition, it may benefit scientists who conduct molecular studies in the areas of chemistry, physics and biology.

Leseprobe

Table of Contents

Cover

Title Page

Copyright

Author Biographies

Preface

Acknowledgments

List of Acronyms

Chapter 1: Introduction

1.1 Time in Chemistry

1.2 Mass Spectrometry

1.3 Time-resolved Mass Spectrometry

1.4 Dynamic Matrices

1.5 Real-time

vs.

Single-point Measurements

1.6 Further Reading

References

Chapter 2: Ion Sources for Time-resolved Mass Spectrometry

2.1 Electron Ionization

2.2 Chemical Ionization

2.3 Atmospheric Pressure Chemical Ionization

2.4 Electrospray Ionization

2.5 Atmospheric Pressure Photoionization

2.6 Desorption/Ionization

2.7 Innovations in the 21st Century

2.8 Concluding Remarks

References

Chapter 3: Mass Analyzers for Time-resolved Mass Spectrometry

3.1 Overview

3.2 Individual Mass Analyzers

3.3 Integrated Analytical Techniques

References

Chapter 4: Interfaces for Time-resolved Mass Spectrometry

4.1 Molecules in Motion

4.2 Time-resolved Mass Spectrometry Systems

4.3 Concluding Remarks

References

Chapter 5: Balancing Acquisition Speed and Analytical Performance of Mass Spectrometry

5.1 Overview

5.2 Spectrum Acquisition Speed

5.3 Relationship between Spectrum Acquisition Time and Mass Spectrometer Performance

References

Chapter 6: Hyphenated Mass Spectrometric Techniques

6.1 Introduction

6.2 Separation Techniques Coupled with Mass Spectrometry

6.3 Ion-mobility Spectrometry

6.4 Other Hyphenated Systems

6.5 Influence of Data Acquisition Speed

6.6 Concluding Remarks

References

Chapter 7: Microfluidics for Time-resolved Mass Spectrometry

7.1 Overview

7.2 Fabrication

7.3 Microreaction Systems

7.4 Hydrodynamic Flow

7.5 Coupling Microfluidics with Mass Spectrometry

7.6 Examples of Applications

7.7 Digital Microfluidics

7.8 Concluding Remarks

References

Chapter 8: Quantitative Measurements by Mass Spectrometry

8.1 The Challenge of Quantitative Mass Spectrometry Measurements

8.2 Selection of Instrument

8.3 Solutions to Quantitative Mass Spectrometry

8.4 Data Treatment

8.5 Concluding Remarks

References

Chapter 9: Data Treatment in Time-resolved Mass Spectrometry

9.1 Overview

9.2 Definition of Terms

9.3 Spectral Patterns

9.4 Mass Accuracy

9.5 Structural Derivation

9.6 Molecule Abundance

9.7 Time-dependent Data Treatment

References

Chapter 10: Applications in Fundamental Studies of Physical Chemistry

10.1 Overview

10.2 Chemical Kinetics

10.3 Chemical Equilibrium

References

Chapter 11: Application of Time-resolved Mass Spectrometry in the Monitoring of Chemical Reactions

11.1 Organic Reactions

11.2 Catalytic Reactions

11.3 Photochemical Reactions

11.4 Concluding Remarks

References

Chapter 12: Applications of Time-resolved Mass Spectrometry in the Studies of Protein Structure Dynamics

12.1 Electrospray Ionization in Protein Studies

12.2 Mass Spectrometry Strategies for Ultra-fast Mixing and Incubation

12.3 Hydrogen/Deuterium Exchange

12.4 Photochemical Methods

12.5 Implementation of Ion-mobility Spectrometry Coupled with Mass Spectrometry

12.6 Concluding Remarks

References

Chapter 13: Applications of Time-resolved Mass Spectrometry in Biochemical Analysis

13.1 Enzymatic Reactions

13.2 Time-resolved Mass Spectrometry in Systems and Synthetic Biology

13.3 Monitoring Living Systems

13.4 Concluding Remarks

References

Chapter 14: Final Remarks

14.1 Current Progress

14.2 Instrumentation

14.3 Software

14.4 Limitations

References

Index

End User License Agreement

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Guide

Cover

Table of Contents

Preface

Begin Reading

List of Illustrations

Chapter 1: Introduction

Figure 1.1 Main components of a mass spectrometer. Reproduced from Kandiah and Urban [29] with permission of The Royal Society of Chemistry

Figure 1.2 (a) Mass spectra obtained by Aston using the early mass spectrometer. Reproduced from Squires [50] with permission of The Royal Society of Chemistry. (b) Mass spectrum of caffeine obtained using a modern ESI-IT mass spectrometer. Courtesy of E.P. Dutkiewicz

Chapter 2: Ion Sources for Time-resolved Mass Spectrometry

Figure 2.1 Ion sources which have been utilized in time-resolved mass spectrometry (TRMS) studies (a dichotomy)

Figure 2.2 Schematic illustration of the EI source. M, analyte; M

+•

, molecular ion; F

+

, fragment ion

Figure 2.3 Plot showing the relationship between the ionization efficiency and the energy of the electron beam used in EI

Figure 2.4 Schematic depiction of the CI source

Figure 2.5 The residence time of the ions in the CI source versus gas pressure. (a) Effective ion source residence time as a function of inlet pressure for three different initial Ar/O

2

, compositions. (b) The ratio of effective ion source residence time to inlet pressure as a function of inlet pressure [19]. Reprinted with permission from Griffith, K.S., Gellene, G.I. (1993) A Simple Method for Estimating Effective Ion Source Residence Time. J. Am. Soc. Mass Spectrom. 4: 787–791. Copyright (1993) American Chemical Society

Figure 2.6 Schematic representation of the APCI source

Figure 2.7 General schematic representation of the processes in ESI-MS [32]. Reprinted with permission from Kebarle, P., Tang, L. (1993) From Ions in Solution to Ions in the Gas Phase. The Mechanism of Electrospray Mass Spectrometry. Anal. Chem. 64: 972A–986A. Copyright (1993) American Chemical Society

Figure 2.8 Time spent on ion formation in ESI. (a) Schematic representation of time history of parent and offspring droplets. Droplet at the top left is a typical parent droplet created near the ESI capillary tip at low flow rates. Evaporation of solvent at constant charge leads to uneven fission. The number beside the droplets gives radius and number of elementary charge N on droplet; corresponds to the time required for evaporative droplet shrinkage to the size where fission occurs. Only the first three successive fissions of a parent droplet are shown. At the bottom right, the uneven fission of an offspring droplet to produce offspring droplet is shown. The timescale is based on (, radius of droplet; , time), which produces only a rough estimate. Inset: Tracing of photograph by Gomez and Tang [36] of droplet undergoing “uneven” fission. Typical droplet loses 2% of its mass, producing some 20 smaller droplets that carry 15% of the parent charge [32]. Reprinted with permission from Kebarle, P., Tang, L. (1993) From Ions in Solution to Ions in the Gas Phase. The Mechanism of Electrospray Mass Spectrometry. Anal. Chem. 64: 972A–986A. Copyright (1993) American Chemical Society. (b) Droplet histories for charged water droplets produced by nanoESI. The first droplet is one of the droplets produced at the spray tip. This parent droplet is followed for three evaporation and fission events. The first generation droplets are shown as well as the fission of one of these to lead to second generation offspring droplets [40]. Reproduced from Peschke, M. et al. (2004) [40] with permission of Springer. Data shown based on experimental results [41] and calculations [40]. (c) In this molecular dynamic simulation, an unfolded protein chain that was initially placed within a Rayleigh-charged water droplet gets ejected via the chain ejection model. Side chains and backbone moieties are represented as beads [42]. Reproduced with permission from Konermann, L., Ahadi, E., Rodriguez, A.D., Vahidi, S. (2013) Unraveling the Mechanism of Electrospray Ionization. Anal. Chem. 85: 2–9. Copyright (2013) American Chemical Society.