Two-Dimensional Optical Spectroscopy discusses the principles and applications of newly emerging two-dimensional vibrational and optical spectroscopy techniques. It provides a detailed account of basic theory required for an understanding of two-dimensional vibrational and electronic spectroscopy. It also bridges the gap between the formal development of nonlinear optical spectroscopy and the application of the theory to explain experimental results. Focusing on time-domain spectroscopy, the book presents detailed discussions on the underlying physics and interpretation methods of a variety of two-dimensional optical spectroscopic methods. It illustrates how novel diagrammatic techniques are useful in graphically describing the associated nonlinear optical transition pathways and involved population or coherence evolutions. The author also explains the basics of quantum dynamics and time-dependent perturbation theories that are required in describing nonlinear optical processes. From the development of the theory to novel applications, this book covers a gamut of topics in this field, including perturbation theory, coherent Raman scattering, pump-probe spectroscopy, photon echo spectroscopy, IR-visible four-wave mixing, and linear and nonlinear optical activity spectroscopy. It shows how to apply the recently developed tools of vibrational and electronic spectroscopy in two dimensions.

Over the last decade, scientific and engineering interests have been shifting from conventional ion mobility spectrometry (IMS) to field asymmetric waveform ion mobility spectrometry (FAIMS). Differential Ion Mobility Spectrometry: Nonlinear Ion Transport and Fundamentals of FAIMS explores this new analytical technology that separates and characterizes ions by the difference between their mobility in gases at high and low electric fields. It also covers the novel topics of higher-order differential IMS and IMS with alignment of dipole direction. The book relates the fundamentals of FAIMS and other nonlinear IMS methods to the physics of gas-phase ion transport. It begins with the basics of ion diffusion and mobility in gases, covering the main attributes of conventional IMS that are relevant to all IMS approaches. Building on this foundation, the author reviews diverse high-field transport phenomena that underlie differential IMS. He discusses the conceptual implementation and first-principles optimization of FAIMS as a filtering technique, emphasizing the dependence of FAIMS performance metrics on instrumental parameters and properties of ion species. He also explores ion reactions in FAIMS caused by field heating and the effects of inhomogeneous electric field in curved FAIMS gaps. Written by an accomplished scientist in the field, this state-of-the-art book supplies the foundation to understand the new technology of nonlinear IMS methods.

Comprehensive, Up-to-Date Coverage of Spectroscopy Theory and its Applications to Biological Systems Although a multitude of books have been published about spectroscopy, most of them only occasionally refer to biological systems and the specific problems of biomolecular EPR (bioEPR). Biomolecular EPR Spectroscopy provides a practical introduction to bioEPR and demonstrates how this remarkable tool allows researchers to delve into the structural, functional, and analytical analysis of paramagnetic molecules found in the biochemistry of all species on the planet. A Must-Have Reference in an Intrinsically Multidisciplinary Field This authoritative reference seamlessly covers all important bioEPR applications, including low-spin and high-spin metalloproteins, spin traps and spin lables, interaction between active sites, and redox systems. It is loaded with practical tricks as well as do's and don'ts that are based on the author's 30 years of experience in the field. The book also comes with an unprecedented set of supporting software designed with simple graphical user interfaces that allow readers to tackle problems they will likely encounter when engaged in spectral analysis. Breaking with convention, the book broaches quantum mechanics from the perspective of biological relevance, emphasizing low-symmetry systems. This is a necessary approach since paramagnets in biomolecules typically have no symmetry. Where key topics related to quantum mechanics are addressed, the book offers a rigorous treatment in a style that is quick-to-grasp for the non expert. Biomolecular EPR Spectroscopy is a practical, all-inclusive reference sure to become the industry standard.

Summarizing our present knowledge of the structures and chemistry of small organic cations in the gas phase, Assigning Structures to Ions in Mass Spectrometry presents the methods necessary for determining gas-phase ion structures. It is a comprehensive resource of background material that is essential for the interpretation and understanding of organic mass spectra. Following a historical introduction of chief discoveries, the book surveys current experimental methods for ion production and separation as well as those designed to reveal qualitative and quantitative aspects of gas-phase ions. It also examines the computational chemistry and theoretical calculations that provide complementary thermochemical, structural, and mechanistic information. Five selected case studies illustrate specific challenges associated with ion structure assignment and thermochemical problems. The last major section of the book contains the data for describing or identifying all ions containing C alone and C with H, O, N, S, P, halogens, and small organic cations. Presenting material written by leading researchers in the field, Assigning Structures to Ions in Mass Spectrometry underscores the importance of understanding the behavior of small organic ions and gas-phase ion chemistry for making new ion structure assignments

A constructive evaluation of the most significant developments in liquid chromatography-mass spectrometry (LC-MS) and its uses for quantitative bioanalysis and characterization for a diverse range of disciplines, Liquid Chromatography-Mass Spectrometry, Third Edition offers a well-rounded coverage of the latest technological developments and applications. As the technology itself has matured into a reliable analytical method over the last 15 years, the most exciting developments occur in LC-MS augments research into new applications. This edition places a stronger emphasis than previous editions on the impact of LC-MS methods, dedicating two-thirds of the text to small-molecule and biomolecular applications such as proteomics, pharmaceutical drug discovery and development, biochemistry, clinical analysis, environmental studies, and natural products research. Supported by the most relevant literature available, each chapter examines how the strategies, technologies, and recent advances-from sample pretreatment to data processing-in LC-MS helped to shape these disciplines. Featuring new chapters and extensive revisions throughout the book, Liquid Chromatography-Mass Spectrometry, Third Edition continues to provide scientists with a definitive guide and reference to the most important principles, strategies, and experimental precedents for applying LC-MS to their research.

Used primarily for characterizing polymers and biological systems, vibrational spectroscopy continues to uncover structural information pertinent to a growing number of applications. Vibrational Spectroscopy of Biological and Polymeric Materials compiles the latest developments in advanced infrared and Raman spectroscopic techniques that are applicable to both polymeric materials and biological compounds. It also presents instrumentation and experimental details that can be used by polymer chemists and biochemists in the design of their own experiments. The text starts by describing the application of static and dynamic FT-IR spectroscopies to liquid crystalline polyurethanes, including a clear exposition of the theory behind the experiments. It discusses the measurement of static and dynamic linear dichroism and stress or strain in both single and multiple fiber composite materials. The book explains the roles of vibrational spectroscopy and the Langmuir-Blodgett technique in the study and preparation of high-quality ultrathin materials. Chapters rich in both theoretical and experimental details describe two-dimensional correlation spectroscopy and vibrational circular dichroism. Biomedically-oriented chapters describe the advances in IR imaging of tissues made possible by focal-plane arrays; as well as the use of ligand-gated FT-IR difference spectroscopy in neuropharmacology, particularly in identifying ligands and modes of action for the large number of membrane receptors recently identified in the human genome. The final chapter discusses the application of time-resolved FT-IR spectroscopy to biological materials, providing a detailed guide to the use of commercial step-scan instrumentation for examining sub-millisecond mechanistic details of photobiological processes. Written by eminent experts in these fields, Vibrational Spectroscopy of Biological and Polymeric Materials is an ideal and practical reference for the broad spectrum of researchers interested in the analysis and integration of biological and polymeric materials.

Describes several specific spectrometric techniques that are very useful in elucidating the fundamental nature of matter: EXAFS--Extended X-Ray Absorption of Fine Structure; SEXAFS--which is EXAFS applied to Surface Phenomena; and XANES--X-Ray Absorption Near Edge Structures. Articles explain the phenomena and describe examples of X-ray absorption applications in several fields, including chemistry, biochemistry, catalysis, amorphous and liquid systems, synchrotron radiation, and surface phenomena. Contributors explain the underlying theory, how to set up X-ray absorption experiments, and how to analyze the details of the resulting spectra. This volume will be of particular interest to physicists, chemists, biologists, and materials scientists.

The new edition of the popular introductory analytical chemistry textbook, providing students with a solid foundation in all the major instrumental analysis techniques currently in use The third edition of Chemical Analysis: Modern Instrumentation Methods and Techniques provides an up-to-date overview of the common methods used for qualitative, quantitative, and structural chemical analysis. Assuming no background knowledge in the subject, this student-friendly textbook covers the fundamental principles and practical aspects of more than 20 separation and spectroscopic methods, as well as other important techniques such as elemental analysis, electrochemistry and isotopic labelling methods. Avoiding technical complexity and theoretical depth, clear and accessible chapters explain the basic concepts of each method and its corresponding instrumental techniques--supported by explanatory diagrams, illustrations, and photographs of commercial instruments. The new edition includes revised coverage of recent developments in supercritical fluid chromatography, capillary electrophoresis, miniaturized sensors, automatic analyzers, digitization and computing power, and more. Offering a well-balanced introduction to a wide range of analytical and instrumentation techniques, this textbook: Provides a detailed overview of analysis methods used in the chemical and agri-food industries, medical analysis laboratories, and environmental sciences Covers various separation methods including chromatography, electrophoresis and electrochromatography Describes UV and infrared spectroscopy, fluorimetry and chemiluminescence, x-ray fluorescence, nuclear magnetic resonance and other common spectrometric methods such atomic or flame emission, atomic absorption and mass spectrometry Includes concise overview chapters on the general aspects of chromatography, sample preparation strategies, and basic statistical parameters Features examples, end-of-chapter problems with solutions, and a companion website featuring PowerPoint slides for instructors Chemical Analysis: Modern Instrumentation Methods and Techniques, Third Edition, is the perfect textbook for undergraduates taking introductory courses in instrumental analytical chemistry, students in chemistry, pharmacy, biochemistry, and environmental science programs looking for information on the techniques and instruments available, and industry technicians working with problems of chemical analysis. Review of Second Edition "An essential introduction to a wide range of analytical and instrumentation techniques that have been developed and improved in recent years." --International Journal of Environmental and Analytical Chemistry

Food contains various compounds and many technologies exist to analyze those molecules of interest. However, the analysis of the spatial distribution of those compounds using conventional technology, such as liquid chromatography-mass spectrometry or gas chromatography-mass spectrometry is difficult. Mass spectrometry imaging (MSI) is a mass spectrometry technique to visualize the spatial distribution of molecules, as biomarkers, metabolites, peptides or proteins by their molecular masses. Despite the fact that MSI has been generally considered a qualitative method, the signal generated by this technique is proportional to the relative abundance of the analyte and so quantification is possible. Mass Spectrometry Imaging in Food Analysis, a volume in the Food Analysis and Properties Series, explains how the novel use of matrix-assisted laser desorption/ionization mass spectrometry imaging (MALDI-MSI) will be an ideal complementary approach. MALDI-MSI is a two-dimensional MALDI-MS technology that can detect compounds in a tissue section without extraction, purification, separation, or labeling. It can be used to visualize the spatial distribution of biomolecules in foods. Features: Explains the novel use of matrix-assisted laser desorption/ionization mass spectrometry imaging in food analysis Describes how MALDI-MSI will be a useful technique for optical quality assurance. Shows how MALDI-MSI detects food contaminants and residues Covers the historical development of the technology While there are a multitude of books on mass spectrometry, none focus on food applications and thus this book is ideally suited to food scientists, food industry personnel engaged in product development, research institutions, and universities active in food analysis or chemical analysis. Also available in the Food Analysis and Properties Series: Food Aroma Evolution: During Food Processing, Cooking, and Aging, edited by Matteo Bordiga and Leo M.L. Nollet (ISBN: 9781138338241) Ambient Mass Spectroscopy Techniques in Food and the Environment, edited by Leo M.L. Nollet and Basil K. Munjanja (ISBN: 9781138505568) Hyperspectral Imaging Analysis and Applications for Food Quality, edited by N.C. Basantia, Leo M.L. Nollet, and Mohammed Kamruzzaman (ISBN: 9781138630796) For a complete list of books in this series, please visit our website at: www.crcpress.com/Food-Analysis--Properties/book-series/CRCFOODANPRO

This book is a comprehensive guide to the theory of optical band shape of guest-molecule-doped crystals, polymers and glasses. The dynamics of a single molecule, measured with the help of a train of photons emitted at random time moments, is a main subject of the book. The dynamics is calculated with the help of quantum-mechanical methods and equations for the density matrix of the system consisting of a single chromophore interacting with light, phonons and non-equilibrium tunneling systems of polymers and glasses. A dynamical theory for one- and two-photon counting methods used in single molecule spectroscopy is presented. Photon bunching and antibunching, jumps of optical lines, and quantum trajectories of various types are further topics addressed. This is the first book to present a detailed theoretical basis for single molecule spectroscopy. It also describes numerous experimental applications of the theory.

Protein phosphorylation analysis is a central theme in current analytical biochemistry, cell biology and systems biology. Due to its versatility, specificity and sensitivity, mass spectrometry has developed into a key technology in this field. A set of minor and major instrumental innovations mean that mass spectrometers now exhibit a level of performance, a stability of operation, a relative ease of use, and productivity, which would once have been hard to imagine. This book guides the reader through this prolific field by presenting a collection of personal views and selected examples which cover all the important principles with a focus on electrospray ionization mass spectrometry. It covers: phosphorylation analysis at the peptide, protein and proteome level; manual and automated data evaluation; phosphopeptide enrichment; quantitative aspects; element mass spectrometry; individual analytical strategies, and hints to useful internet resources. This book provides students, graduate students, post-Docs and senior scientists from related areas with a better understanding on molecular protein phosphorylation analysis. Its highest aim is to strengthen the reader's ability to develop a personal, well-founded opinion on original manuscripts published in this field.

The first hands-on guide to XRD and XRF sampling and specimen preparation

Systematic errors from poor sampling and improper specimen preparation can easily render X-ray diffraction (XRD) and X-ray fluorescence (XRF) data of questionable use for analysis. But, until now, the practical information that can help to reduce these errors has never been readily available in one volume.

This book fills a vital gap in the literature, bringing together a wealth of material previously available only in workbooks, company manuals, and other inside sources. It provides detailed coverage of the major tasks involved in X-ray analysis — complete with theory, step-by-step methods, equipment suggestions, and problem-solving tips.

With a full complement of tools and techniques, this comprehensive guide helps both beginners and experienced analysts to make the best decision on sample treatment and get accurate XRD and XRF results—saving valuable time, money, and effort.

Covers X-ray techniques for analyzing biological, geological, metallic, ceramic, and other materials

• Addresses all aspects of specimen preparation, including handling unusual or very small samples, liquids and solutions, and more
• Features special chapters on specimen preparation equipment and XRF standards
• Contains useful bibliography and helpful references.

Laser induced breakdown spectroscopy (LIBS) is basically an emission spectroscopy technique where atoms and ions are primarily formed in their excited states as a result of interaction between a tightly focused laser beam and the material sample. The interaction between matter and high-density photons generates a plasma plume, which evolves with time and may eventually acquire thermodynamic equilibrium. One of the important features of this technique is that it does not require any sample preparation, unlike conventional spectroscopic analytical techniques. Samples in the form of solids, liquids, gels, gases, plasmas and biological materials (like teeth, leaf or blood) can be studied with almost equal ease. LIBS has rapidly developed into a major analytical technology with the capability of detecting all chemical elements in a sample, of real- time response, and of close-contact or stand-off analysis of targets. The present book has been written by active specialists in this field, it includes the basic principles, the latest developments in instrumentation and the applications of LIBS . It will be useful to analytical chemists and spectroscopists as an important source of information and also to graduate students and researchers engaged in the fields of combustion, environmental science, and planetary and space exploration.
* Recent research work
* Possible future applications
* LIBS Principles

This volume comprises the proceedings of the 15th International Mass Spectrometry Conference held in Barcelona, attended by over 1100 registered delegates from 38 countries. Because the applications of mass spectrometry to biochemistry, biology and medicine have become a very important source of activity in the field these areas are very well represented in the content of this volume. However the importance of fundamental research and instrumental and methodology developments to all applications is also highlighted.

The book is divided into five sections:

· Fundamentals

· Biological/Biochemical Applications,

· Instrumentation and Ionization

· Analytical Organic Mass Spectrometry

· Inorganic Mass Spectrometry

These five sections consist of full papers from the excellent plenary and keynote speakers together with abstracts of more than 300 oral and poster contributions from the total of 701 presented at the conference. The selection reflects the present state-of-the art in the field of mass spectrometry.

ICOLS features the latest developments in the area of laser spectroscopy and related topics in atomic, molecular, and optical physics and other disciplines. The talks covered a broad range of exciting physics, such as precision tests of fundamental symmetries with atoms and molecules, atomic clocks, quantum many-body physics with ultra-cold atoms, atom interferometry, quantum information science with photons and ions, quantum optics, and ultra-fast atomic and molecular dynamics.The conference program comprised 14 sessions with 9 keynote addresses, 25 invited talks, and 3 hot topic talks. The speakers came from 15 different countries. Ever since the ICOLS conference series originated in 1973, its proceedings have been highly valued by many for capturing important developments in the field and offering the room to represent various aspects of specific research topics. The present volume contains some of the invited talks delivered at the conference.

In virtually all types of experiments in which a response is analyzed as a function of frequency (e. g., a spectrum), transform techniques can significantly improve data acquisition and/or data reduct ion. Research-level nuclear magnet ic resonance and infra-red spectra are already obtained almost exclusively by Fourier transform methods, because Fourier transform NMR and IR spectrometers have been commercially available since the late 1960.s. Similar transform techniques are equally valuable (but less well-known) for a wide range of other chemical applications for which commercial instruments are only now becoming available: for example, the first corrmercial Fourier transform mass spectrometer was introduced this year (1981) by Nicolet Instrument Corporation. The purpose of this volume is to acquaint practicing chemists with the basis, advantages, and applica of Fourier, Hadamard, and Hilbert transforms in chemistry. For tions almost all chapters, the author is the investigator who was the first to apply such methods in that field. The basis and advantages of transform techniques are described in Chapter 1. Many of these aspects were understood and first applied by infrared astronomers in the 1950.s, in order to improve the otherwise unacceptably poor signal-to-noise ratio of their spec tra. However, the computations required to reduce the data were painfully slow, and required a 1 arge computer."

Nuclear magnetic resonance (NMR) is widely used across many fields of science because of the rich data it produces, and some of the most valuable data come from studies of nuclear spin relaxation in solution. The first edition of this book, published more than a decade ago, provided an accessible and cohesive treatment of the field. The present second edition is a significant update, covering important new developments in recent years. Collecting relaxation theory, experimental techniques, and illustrative applications into a single volume, this book clarifies the nature of the phenomenon, shows how to study it and explains why such studies are worthwhile. Coverage ranges from basic to rigorous theory and from simple to sophisticated experimental methods. Topics include cross-relaxation, multispin phenomena, relaxation studies of molecular dynamics and structure and special topics such as relaxation in systems with quadrupolar nuclei, in paramagnetic systems and in long-living spin states. Avoiding overly demanding mathematics, the authors explain spin relaxation in a manner that anyone with a familiarity with NMR can follow. The focus is on illustrating and explaining the physical nature of relaxation phenomena. Nuclear Spin Relaxation in Liquids: Theory, Experiments and Applications, 2nd Edition, provides useful supplementary reading for graduate students and is a valuable reference for NMR spectroscopists, whether in chemistry, physics or biochemistry.

This book details chiroptical spectroscopic methods: electronic circular dichroism (ECD), optical rotatory dispersion (ORD), vibrational circular dichroism (VCD), and vibrational Raman optical activity (VROA). For each technique, the text presents experimental methods for measurements and theoretical methods for analyzing the experimental data. It also includes a set of experiments that can be adopted for undergraduate teaching laboratories. Each chapter is written in an easy-to-follow format for novice readers, with necessary theoretical formalism in appendices for advanced readers.

This book offers an elementary introduction to optical spectroscopy with polarized light. It is written at a level suitable for undergraduate students in chemistry and undergraduate or graduate students in related disciplines such as biochemistry, biology, chemical engineering and materials science. It emphasizes the qualitative concepts and deemphasizes mathematics, yet provides sufficient information and practical hints for experiments.
With this book in hand, anyone who can measure an ordinary infrared, ultraviolet or visible absorption or fluorescence emission spectrum can measure a polarized one as well and learn far more about the sample.

NMR spectroscopy has undergone a revolution in recent years with the advent of several new methods overcoming the problems of sensitivity and resolution. Recent developments in biotechnology have made it easier and economical to introduce 13C, 15N and 2H into proteins and nucleic acids. At the same time, there has been an explosion in the number of NMR experiments that utilize such isotope labeled samples. Thus, a combination of isotopic labeling and multidimensional, multinuclear NMR has opened up new avenues for structural studies of proteins, nucleic acids and their complexes.

This book will focus on recent developments in isotope labeling methods for structural studies of small molecules, peptides, proteins and nucleic acids. The aim of the book is to serve as a compendium of isotope labeling for the biomolecular NMR community providing comprehensive coverage of the existing methods and latest developments along with protocols and practical hints on the various experimental aspects. The book will cover a wide range of topics in isotope labeling under one title including emerging areas of metabolonomics and solid state NMR.

Selecting illustrative examples from the recent literature, this reference studies the underlying principles and physics of a wide range of spectroscopic techniques utilized in the pharmaceutical sciences and demonstrates various applications for each method analyzed in the text-showing how knowledge of the mechanisms of spectroscopic phenomena may facilitate more advanced technologies in the field.

Protein NMR Spectroscopy combines a comprehensive theoretical treatment of NMR spectroscopy with an extensive exposition of the experimental techniques applicable to proteins and other biological macromolecules in solution. Beginning with simple theoretical models and experimental techniques, Protein NMR Spectroscopy develops the complete repertoire of theoretical principles and experimental techniques necessary for understanding and implementing the most sophisticated NMR experiments.
Important new techniques and applications of NMR spectroscopy have emerged since the first edition of this extremely successful book was published in 1996. The second edition includes new sections describing measurement and use of residual dipolar coupling constants for structure determination, TROSY and deuterium labeling for application to large macromolecules, and experimental techniques for characterizing conformational dynamics. In addition, the treatments of instrumentation and signal acquisition, field gradients, multidimensional spectroscopy, and structure calculation are updated and enhanced.
Protein NMR Spectroscopy is written as a graduate-level textbook and will be of interest to biochemists, chemists, biophysicists, and structural biologists who utilize NMR spectroscopy or who wish to understand the latest developments in this field.
. Provides an understanding of the theoretical principles important for biological NMR spectroscopy
. Demonstrates how to implement, optimize and troubleshoot modern multi-dimensional NMR experiments
. Allows for the capability of designing effective experimental protocols for investigations of protein structures and dynamics
. Includes a comprehensive set of example NMR spectra of ubiquitin provides a reference for validation of experimental methods"

Spectroscopic Techniques and Hindered Molecular Motion presents a united, theoretical approach to studying classical local thermal motion of small molecules and molecular fragments in crystals by spectroscopic techniques. Mono- and polycrystalline case studies demonstrate performance validity. The book focuses on small molecules and molecular fragments, such as N2, HCl, CO2, CH4, H2O, NH4, BeF4, NH3, CH2, CH3, C6H6, SF6, and other symmetrical atomic formations, which exhibit local hindered motion in molecular condensed media: molecular and ionic crystals, molecular liquids, liquid crystals, polymeric solids, and biological objects. It reviews the state of studying the hindered molecular motion (HMM) phenomenon and the experimental works on the basis of the latest theoretical research. Case Studies Physical models of hindered molecular motion General solution of the stochastic problem for the hindered molecular motion in crystals Formulae of the angular autocorrelation function symmetrized on the crystallographic point symmetry groups Formulae of the spectral line shapes concerning the dielectric, infrared, Raman, nuclear magnetic relaxation, and neutron scattering spectroscopy in the presence of the hindered molecular motion Experimental probation of the theoretical outcomes Proton relaxation in three-atomic molecular fragments undergoing axial symmetry hindered motion Structural distortion in the ordered phase of crystalline ammonium chloride Organic compounds, polymers, pharmaceutical products, and biological systems consist of the molecular fragments, which possess rotational or conformational degrees of freedom or an atomic exchange within the fragme

Laser spectroscopy has been perfected over the last fifteen years to become a precise tool for the investigation of highly vibrationally excited molecules. Intense infrared laser radiation permits both the multiple-photon resonant excitation and the dissociation of polyatomic molecules. In this book, the latest results of some of the foremost Soviet researchers are published for the first time in the West. Laser Spectroscopy of Highly Vibrationally Excited Molecules contains a comprehensive study of both the experimental and theoretical aspects of the basic photophysical interactions that occur in these processes. The book first focuses on the nonlinear interaction between the resonant vibrational mode and the intense infrared field and then examines the nonlinear interaction between the vibrational modes themselves due to anharmonicity. These interrelated processes determine all the characteristics of polyatomic molecules in an infrared field. The book also discusses related phenomena such as spectra broadening, optical resonance, photon echoes, and dynamical chaos. It includes examples of multiple-photon resonant excitation such as the excitation of OsO4 by CO^O2 laser radiation, which is detected by the visible luminescence that results. This book will be of great interest to researchers and postgraduate students in infrared laser spectroscopy and the laser chemistry of molecules and applications of isotope separation.