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Nuclear Magnetic Resonance spectroscopy is a dynamic way for scientists of all kinds to investigate the physical, chemical, and biological properties of matter. Its many applications make it a versatile tool previously subject to monolithic treatment in reference-style texts. Based on a course taught for over ten years at Brandeis University, this is the first textbook on NMR spectroscopy for a one-semester course or self-instruction. In keeping with the authors' efforts to make it a useful textbook, they have included problems at the end of each chapter. The book not only covers the latest developments in the field, such as GOESY (Gradient Enhanced Overhauser Spectroscopy) and multidimensional NMR, but includes practical examples using real spectra and associated problem sets. Assuming the reader has a background of chemistry, physics and calculus, this textbook will be ideal for graduate students in chemistry and biochemistry, as well as biology, physics, and biophysics. NMR for Physical and Biological Scientists will also be useful to medical schools, research facilities, and the many chemical, pharmaceutical, and biotech firms that offer in-house instruction on NMR spectroscopy.
For those wanting to become rapidly acquainted with specific areas of NMR, this title provides unrivalled scope of coverage. Applications of NMR span a wide range of scientific disciplines, from physics to biology to medicine. Each volume in this series comprises a combination of reports offering comprehensive coverage of the literature on this topic. For those wanting to become rapidly acquainted with specific areas of NMR this title provides unrivalled scope of coverage. Seasoned practitioners of NMR will find this an invaluable source of current methods and applications. Reviews include literature published from June 2007 to May 2008.
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.
During teaching NMR to students and researchers, we felt the need for a text-book which can cover modern trends in the application of NMR to biological systems. This book covers the entire area of NMR in Biological Sciences (Biomolecules, cells and tissues, animals, plants and drug design). As well as being useful to researchers, this is an excellent book for teaching a course on NMR in Biological Systems.
This book presents a critical assessment of progress on the use of nuclear magnetic resonance spectroscopy to determine the structure of proteins, including brief reviews of the history of the field along with coverage of current clinical and in vivo applications. The book, in honor of Oleg Jardetsky, one of the pioneers of the field, is edited by two of the most highly respected investigators using NMR, and features contributions by most of the leading workers in the field. It will be valued as a landmark publication that presents the state-of-the-art perspectives regarding one of today's most important technologies.
The technique of nuclear magnetic resonance (NMR) spectroscopy is an important tool in biochemistry and biophysics for the understanding of the structure and ultimately, the function of biomolecules. This textbook explains the salient features of biological NMR spectroscopy to undergraduates and postgraduates taking courses in NMR, biological NMR, physical biochemistry, and biophysics. Unlike other books in the general field of NMR (except the advanced treatises), the approach here is tointroduce and make use of quantum mechanical product operators as well as the classical vector method of explaining the bewildering array of pulse sequences available today. The book covers two- dimensional, three- dimensional, and four- dimensional NMR and their application to protein and DNA structure determination. A unique feature is the coverage of the biological aspects of solid- state NMR spectroscopy. The author provides many selected examples from the research literature, illustratingthe applications of NMR spectroscopy to biological proteins.
In-cell NMR spectroscopy is a relatively new field. Despite its short history, recent in-cell NMR-related publications in major journals indicate that this method is receiving significant general attention. This book provides the first informative work specifically focused on in-cell NMR. It details the historical background of in-cell NMR, host cells for in-cell NMR studies, methods for in-cell biological techniques and NMR spectroscopy, applications, and future perspectives. Researchers in biochemistry, biophysics, molecular biology, cell biology, structural biology as well as NMR analysts interested in biological applications will all find this book valuable reading.
Although nuclear magnetic resonance is perhaps best known for its spectacular utility in medical tomography, its potential applicability to fields such as biology, materials science, and chemical physics is being increasingly recognized as laboratory NMR spectrometers are adapted to enable small scale imaging. This excellent introduction to the subject explores principles and common themes underlying two key variants of NMR microscopy, and provides many examples of their use. Methods discussed are not only important to fundamental biological and physical research, but have applications to a wide variety of industries, including those concerned with petrochemicals, polymers, biotechnology, food processing, and natural product processing. The wide range of scientists interested in NMR microscopy will want to own a copy of this book.
NMR Probeheads for Biophysical and Biomedical Experiments 2nd Edition is essential reading for anyone in the field of NMR or MRI, from students to medical or biological scientists performing experiments under certain physical and/or geometrical conditions, unattainable by conventional or available probes. The material guides the reader through the most basic and comprehensive stages in accomplishing a correct probe design, from a very basic oscillating circuit to much more elaborate designs.This new edition has been revised and updated to include a chapter dedicated to RF components, which are commonly used for probes realization and their frequency-dependent characteristics. Another completely revised chapter concerns the multiple coil systems and discusses arrays coils, different decoupling methods, and some principles for interfacing coils with low-noise preamplifiers. The principles of linear circuit analysis are presented in a dedicated chapter. Last but not least, accompanying files containing updated software for probe design have been made available from the publisher's website.
From complex structure elucidation to biomolecular interactions - this applicationoriented textbook covers both theory and practice of modern NMR applications. Part one sets the stage with a general description of NMR introducing important parameters such as the chemical shift and scalar or dipolar couplings. Part two describes the theory behind NMR, providing a profound understanding of the involved spin physics, deliberately kept shorter than in other NMR textbooks, and without a rigorous mathematical treatment of all the physico-chemical computations. Part three discusses technical and practical aspects of how to use NMR. Important phenomena such as relaxation, exchange, or the nuclear Overhauser effects and the methods of modern NMR spectroscopy including multidimensional experiments, solid state NMR, and the measurement of molecular interactions are the subject of part four. The final part explains the use of NMR for the structure determination of selected classes of complex biomolecules, from steroids to peptides or proteins, nucleic acids, and carbohydrates. For chemists as well as users of NMR technology in the biological sciences.