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.

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

New insights into modern medicine and systems biology are enabled by innovative protocols and advanced technologies in mass spectrometry-based proteomics. This volume details new pipelines, workflows, and ways to process data that allow for new frontiers in proteomics to be pushed forward. With applications to biomarker discovery, interactions between proteins, between biological systems, dynamics of post-translational modifications among others, new protocols have been developed and iteratively refined to probe the endless complexity of the proteome in ever greater details. This volume deals with methods for data dependent and data independent mass spectrometry analyses. Valuable, first-hand information is provided from designing experiments, sample preparation and analysis, exploitation of public datasets and carrying out reproducible data pipelines, using modern computational tools such as Galaxy or Jupyter. Written in the highly successful Methods in Molecular Biology series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls. Authoritative and cutting-edge, Mass Spectrometry of Proteins: Methods and Protocols aims to ensure successful results in the further study of this vital field.

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.

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.

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.

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 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.

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.

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.

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."

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.

Over the past decade, a myriad of techniques have shown that solid-state nuclear magnetic resonance (NMR) can be used in a broad spectrum of applications with exceptionally impressive results. Solid-state NMR results can yield high-resolution details on the structure and function of many important biological solids, including viruses, fibril-forming molecules, and molecules embedded in the cell membrane. Filling a void in the current literature, NMR Spectroscopy of Biological Solids examines all the recent developments, implementation, and interpretation of solid-state NMR experiments and the advantages of applying them to biological systems. The book emphasizes how these techniques can be used to realize the structure of non-crystalline systems of any size. It explains how these isotropic and anisotropic couplings interactions are used to determine atomic-level structures of biological molecules in a non-soluble state and extrapolate the three-dimensional structure of membrane proteins using magic-angle spinning (MAS). The book also focuses on the use of multidimensional solid-state NMR methods in the study of aligned systems to provide basic information about the mechanisms of action of a variety of biologically active molecules. Addressing principles, methods, and applications, this book provides a critical selection of solid-state NMR methods for solving a wide range of practical problems that arise in both academic and industrial research of biomolecules in the solid state. NMR Spectroscopy of Biological Solids is a forward-thinking resource for students and researchers in analytical chemistry, bioengineering, material sciences, and structural genomics.

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

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.

This volume details the principles and instrumentation of gas chromatography-mass spectrometry (CG-MS), and outlines industrial, environmental, pharmaceutical, clinical, toxicological, forensic and food-related applications, revealing findings from the laboratories of 40 contributing scientists around the world using GC-MS in practice. It describes upstream and downstream applications of GC-MS in the petroleum industry and identifies chlorinated compounds in the environment with quadrupole ion-trap technology and high-resolution sector instruments.

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.

Stimulated by the increasing importance of chiral molecules as pharmaceuticals and the need for enantiomerically pure drugs, techniques in chiral chemistry have been expanded and refined, especially in the areas of chromatography, asymmetric synthesis, and spectroscopic methods for chiral molecule structural characterization. In addition to synthetic chiral molecules, naturally occurring molecules, which are invariably chiral and generally enantiomerically enriched, are of potential interest as leads for new drugs. VCD Spectroscopy for Organic Chemists discusses the applications of vibrational circular dichroism (VCD) spectroscopy to the structural characterization of chiral organic molecules. The book provides all of the information about VCD spectroscopy that an organic chemist needs in order to make use of the technique. The authors, experts responsible for much of the existing literature in this field, discuss the experimental measurement of VCD and the theoretical prediction of VCD. In addition, they evaluate the advantages and limitations of the technique in determining molecular structure. Given the availability of commercial VCD instrumentation and quantum chemistry software, it became possible in the late 1990s for chemists to use VCD in elucidating the stereochemistries of chiral organic molecules. This book helps organic chemists become more aware of the utility of VCD spectroscopy and provides them with sufficient knowledge to incorporate the technique into their own research.

Second Edition provides up-to-the-minute discussions on the application of mass spectrometry to the biological sciences. Shows how and why experiments are performed and furnishes details to facilitate duplication of results.

A teaching tool intended to complement existing books on the theory of materials science, metallurgy, and electron microscopy, this text focuses on metals and alloys. It visualizes key structural elements common to crystalline materials, including crystal lattice imperfections, along with the principles and steps involved in the microstructure development in metallic materials under external influences. Designed as an atlas, Microstructure of Metals and Alloys contains a collection of carefully selected original transmission electron microscope (TEM) micrographs taken by the authors. These images demonstrate typical crystal lattice defects, elements of the microstructure of metals and alloys, and the basic processes occurring to the crystal structure during plastic deformation, polygonization, recrystallization, and rapid solidification. The book is organized into six chapters. Each deals with a particular problem in the field of physical metallurgy, and begins with a description of the basic concept and terms. These descriptions enable readers to achieve a better understanding of the essential issues relevant to specific challenges. Providing comprehensive, illustrative coverage of the basic topics in materials science, this important work emphasizes fundamental principles over specific materials, in a manner that is fully consistent with the contemporary tendency in materials science teaching.

Remarkable developments in the spectroscopy field regarding ultrashort pulse generation have led to the possibility of producing light pulses ranging from 50 to5 fs and frequency tunable from the near infrared to the ultraviolet range. Such pulses enable us to follow the coupling of vibrational motion to the electronic transitions in molecules and solids in real time. Detailing these advanced developments, as well as the fundamental methods and tools of vibrational spectroscopy, Coherent Vibrational Dynamics providesresearchers and students with a uniquely comprehensive resource. With the contributions of pioneering scientists, this seminal volume - * Outlines the principles and tools used on time-domain vibrational spectroscopy and provides a general introduction to the subject of coherent phonons * Describes the modern methods for tunable ultrashort pulse generation from infrared to visible-UV * Reviews coherent vibrational dynamics in small molecules in liquids (hydrogen bonds), and in carbon based conjugated materials (polyenes, carotenoids, and semiconducting polymers) * Explores phonon dynamics in semiconductors (bulk and heterostructures) and in quasi-one-dimensional systems Supplemented with a great number of references, and covering fundamental as well advanced topics, this text provides a valuable reference for both graduate students and senior researchers investigating materials in physics, chemistry, and biology. It is also an excellent starting point for those who want to pursue research in the field of ultrafast optics and spectroscopy.