This book is about pulse nuclear magnetic resonance (NMR), with its techniques, the information to be obtained, and practical advice on performing experiments. The emphasis is on the motivation and physical ideas underlying NMR experiments and the actual techniques, including the hardware used. The level is generally suitable for those to whom pulse NMR is a new technique, be they students in chemistry or physics on the one hand and research workers in biology, geology, or agriculture, on the other. The book can be used for a senior or first year graduate course where it could supplement the standard NMR texts.
This work-book will guide you safely, in step-by-step descriptions, through every detail of the NMR experiments within, beginning with 1D routine experiments and ending with a series of advanced 3D experiments on a protein: ? Which experiment can best yield the desired information? ? How must the chosen experiment be performed? ? How does one read the required information from the spectrum? ? How does this particular pulse sequence work? ? Which other experiments give similar information? This third edition of the book, following its two highly successful predecessors, has been revised and expanded to 206 experiments. They are organized in 15 chapters, covering test procedures and routine spectra, variable temperature measurements, the use of auxiliary reagents, 1D multipulse experiments, spectra of heteronuclides, and the application of selective pulses. The second and third dimensions are introduced using pulsed field gradients, and experiments on solid state materials are described. A key part describes 3D experiments on the protein ubiquitin with 76 amino acids. What is new in this third edition? 1. 24 new experiments have been inserted into the 14 chapters that were in the 2nd edition, e.g., alpha/beta-SELINCOR-TOCSY, WET, DOSY, ct-COSY, HMSC, HSQC with adiabatic pulses, HETLOC. J-resolved HMBC, (1,1)- and (1,n)-ADEQUATE, STD, REDOR, and HR-MAS. 2. 20 new protein NMR experiments have been specially devised and are collected in the newly added Chapter 15, ProteinNMR, for which one needs a special model sample: fully 13C- and 15N-labeled human ubiquitin. Techniques used include the constant time principle, the PEP method, filters, gradient selection, and the echo/anti-echo procedure. The guide has been written by experts in this field, following the principle of learning by doing: all the experiments have been specially performed for this book, exactly as described and shown in the spectra that are reproduced. Being a reference source and work-book for the NMR laboratory as well as a textbook, it is a must for every scientist working with NMR, as well as for students preparing for their laboratory courses
From the initial observation of proton magnetic resonance in water and in paraffin, the discipline of nuclear magnetic resonance has seen unparalleled growth as an analytical method. Modern NMR spectroscopy is a highly developed, yet still evolving, subject which finds application in chemistry, biology, medicine, materials science and geology. In this book, emphasis is on the more recently developed methods of solution-state NMR applicable to chemical research, which are chosen for their wide applicability and robustness. These have, in many cases, already become established techniques in NMR laboratories, in both academic and industrial establishments. A considerable amount of information and guidance is given on the implementation and execution of the techniques described in this book.
Combines clear and concise discussions of key NMR concepts with succinct and illustrative examples Designed to cover a full course in Nuclear Magnetic Resonance (NMR) Spectroscopy, this text offers complete coverage of classic (one-dimensional) NMR as well as up-to-date coverage of two-dimensional NMR and other modern methods. It contains practical advice, theory, illustrated applications, and classroom-tested problems; looks at such important ideas as relaxation, NOEs, phase cycling, and processing parameters; and provides brief, yet fully comprehensible, examples. It also uniquely lists all of the general parameters for many experiments including mixing times, number of scans, relaxation times, and more. Nuclear Magnetic Resonance Spectroscopy: An Introduction to Principles, Applications, and Experimental Methods, 2nd Edition begins by introducing readers to NMR spectroscopy - an analytical technique used in modern chemistry, biochemistry, and biology that allows identification and characterization of organic, and some inorganic, compounds. It offers chapters covering: Experimental Methods; The Chemical Shift; The Coupling Constant; Further Topics in One-Dimensional NMR Spectroscopy; Two-Dimensional NMR Spectroscopy; Advanced Experimental Methods; and Structural Elucidation. Features classical analysis of chemical shifts and coupling constants for both protons and other nuclei, as well as modern multi‐pulse and multi-dimensional methods Contains experimental procedures and practical advice relative to the execution of NMR experiments Includes a chapter-long, worked-out problem that illustrates the application of nearly all current methods Offers appendices containing the theoretical basis of NMR, including the most modern approach that uses product operators and coherence-level diagrams By offering a balance between volumes aimed at NMR specialists and the structure-determination-only books that focus on synthetic organic chemists, Nuclear Magnetic Resonance Spectroscopy: An Introduction to Principles, Applications, and Experimental Methods, 2nd Edition is an excellent text for students and post-graduate students working in analytical and bio-sciences, as well as scientists who use NMR spectroscopy as a primary tool in their work.
This book describes the advanced developments in methodology and applications of NMR spectroscopy to life science and materials science. Experts who are leaders in the development of new methods and applications of life and material sciences have contributed an exciting range of topics that cover recent advances in structural determination of biological and material molecules, dynamic aspects of biological and material molecules, and development of novel NMR techniques, including resolution and sensitivity enhancement. First, this book particularly emphasizes the experimental details for new researchers to use NMR spectroscopy and pick up the potentials of NMR spectroscopy. Second, the book is designed for those who are involved in either developing the technique or expanding the NMR application fields by applying them to specific samples. Third, the Nuclear Magnetic Resonance Society of Japan has organized this book not only for NMR members of Japan but also for readers worldwide who are interested in using NMR spectroscopy extensively.
NMR spectroscopy has proven to be a powerful technique to study the structure and dynamics of biological macromolecules. Fundamentals of Protein NMR Spectroscopy is a comprehensive textbook that guides the reader from a basic understanding of the phenomenological properties of magnetic resonance to the application and interpretation of modern multi-dimensional NMR experiments on 15N/13C-labeled proteins. Beginning with elementary quantum mechanics, a set of practical rules is presented and used to describe many commonly employed multi-dimensional, multi-nuclear NMR pulse sequences. A modular analysis of NMR pulse sequence building blocks also provides a basis for understanding and developing novel pulse programs. This text not only covers topics from chemical shift assignment to protein structure refinement, as well as the analysis of protein dynamics and chemical kinetics, but also provides a practical guide to many aspects of modern spectrometer hardware, sample preparation, experimental set-up, and data processing. End of chapter exercises are included to emphasize important concepts. Fundamentals of Protein NMR Spectroscopy not only offer students a systematic, in-depth, understanding of modern NMR spectroscopy and its application to biomolecular systems, but will also be a useful reference for the experienced investigator.
This primer describes the range of NMR techniques commonly used in modern research, and explains how these experiments actually work, giving a unique perspective on this powerful experimental tool.
The idea that a long-lived form of spin order, namely singlet order, can be prepared from nuclear spin magnetisation first emerged in 2004. The unusual properties of singlet order–its long lifetime and the fact that it is NMR silent but interconvertible into other forms of NMR active order—make it a ‘smart tag’ that can be used to store information for a long time or through distant space points. It is not unexpected then, that since its first appearance, this idea has caught the attention of research groups interested in exploiting this form of order in different fields of research spanning from biology to materials science and from hyperpolarisation to quantum computing. This first book on the subject gives a thorough description of the various aspects that affect the development of the topic and details the interdisciplinary applications. The book starts with a section dedicated to the basic theories of long-lived spin order and then proceeds with a description of the state-of-the-art experimental techniques developed to manipulate singlet order. It then concludes by covering the generalization of the concept of singlet order by introducing and discussing other forms of long-lived spin order.
The field of Nuclear Magnetic Resonance (NMR) has developed at a fascinating pace during the last decade. It always has been an extremely valuable tool to the organic chemist by supplying molecular "finger print" spectra at the atomic level. Unfortunately the high resolution achievable in liquid solutions could not be obtained in solids and physicists and physical chemists had to live with unresolved lines open to a wealth of curve fitting procedures and a vast amount of speculations. High resolution NMR in solids seemed to be a paradoxon. Broad structure less lines are usually encountered when dealing with NMR in solids. Only with the recent advent of mUltiple pulse, magic angle, cross-polarization, two-dimen sional and multiple-quantum spectroscopy and other techniques during the last decade it became possible to resolve finer details of nuclear spin interactions in solids. I have felt that graduate students, researchers and others beginning to get involved with these techniques needed a book which treats the principles, theo retical foundations and applications of these rather sophisticated experimental techniques. Therefore I wrote a monograph on the subject in 1976. Very soon new ideas led to the developement of "two-dimensional spectroscopy" and "multiple-quantum spectroscopy", topics which were not covered in the first edition of my book. Moreover an exponential growth of literature appeared in this area of research leaving the beginner in an awkward situation of tracing back from a current article to the roots of the experiment.
Solid State NMR A thorough and comprehensive textbook covering the theoretical background, experimental approaches, and major applications of solid-state NMR spectroscopy Nuclear Magnetic Resonance (NMR) spectroscopy is a powerful non-destructive technique capable of providing information about the molecular structure and dynamics of molecules. Alongside solution-state NMR, a well-established technique to study chemical structures and investigate physico-chemical properties of molecules in solutions, solid-state NMR (SSNMR) offers many exciting possibilities for the analysis of solid and soft materials across scientific fields. SSNMR shows unique capabilities for a detailed investigation of structural and dynamic properties of materials over wide space and time ranges. For this reason, and thanks to significant advances in the past several years, the application of SSNMR to materials is rapidly increasing in disciplines such as chemistry, physics, and materials and life sciences. Solid State NMR: Principles, Methods, and Applications offers a systematic introduction to the theory, methodological concepts, and major experimental methods of SSMR spectroscopy. Exploring the unique potential of SSNMR for the structural and dynamic characterization of soft and either amorphous or crystalline solid materials, this comprehensive textbook provides foundational knowledge and recent developments of SSNMR, covering physical and theoretical background, experimental methods, and applications to pharmaceuticals, polymers, inorganic and hybrid materials, liquid crystals, and model membranes. Written by two expert authors to ensure a clear and consistent presentation of the subject, this textbook: Includes a brief introduction to the historical aspects and broad theoretical background of solid-state NMR spectroscopy Provides helpful illustrations to explain the various SSNMR concepts and methods Features accessible descriptive text with self-consistent use of quantum mechanics Covers the experimental aspects of SSNMR spectroscopy and in particular a description of many useful pulse sequences Contains references to relevant literature Solid State NMR: Principles, Methods, and Applications is the ideal textbook for university courses on SSNMR, advanced spectroscopies, and a valuable single-volume reference for spectroscopists, chemists, and researchers in the field of materials.
