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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.
Protein NMR Spectroscopy: Principles and Practice combines a comprehensive theoretical treatment of high resolution NMR spectroscopy with an extensive exposition of the experimental techniques applicable to proteins and other biological macromolecules. Beginning with simple theoretical models and experimental techniques, Protein NMR Spectroscopy: Principles and Practice develops the complete repertoire of theoretical principals and experimental practices necessary for understanding and implementing the most sophisticated NMR experiments. Protein NMR Spectroscopy: Principles and Practice is written as a graduate-level textbook and will be of particular interest to biochemists, chemists, biophysicists, and structural biologists who utilize NMR spectroscopy as a research tool or who wish to remain abreast of the latest developments in this increasingly important area. * Special Features: * First book to combine detailed NMR theory discussions with experimental applications to biomolecules. * All the theory required to understand these experiments and others. * Easy to follow progression from a fundamental level to an advanced level. * Theory of NMR and practical applications for biomolecular investigations presented. * Theory applied to very practical situations. * Comprehensive treatment of different "levels" of theory from simple ideas to density matrix analysis and operator practices. * Comprehensive description of multi dimensional NMR experiments as applied to unlabeled, 15N-labeled and doubly (13C/15N) labeled proteins.
Nuclear Magnetic Resonance is a powerful tool, especially for the identification of 1 13 hitherto unknown organic compounds. H- and C-NMR spectroscopy is known and applied by virtually every synthetically working Organic Chemist. Con- quently, the factors governing the differences in chemical shift values, based on chemical environment, bonding, temperature, solvent, pH, etc. , are well understood, and specialty methods developed for almost every conceivable structural challenge. Proton and carbon NMR spectroscopy is part of most bachelors degree courses, with advanced methods integrated into masters degree and other graduate courses. In view of this universal knowledge about proton and carbon NMR spectr- copy within the chemical community, it is remarkable that heteronuclear NMR is still looked upon as something of a curiosity. Admittedly, most organic compounds contain only nitrogen, oxygen, and sulfur atoms, as well as the obligatory hydrogen and carbon atoms, elements that have an unfavourable isotope distribution when it comes to NMR spectroscopy. Each of these three elements has a dominant isotope: 14 16 32 16 32 N (99. 63% natural abundance), O (99. 76%), and S (95. 02%), with O, S, and 34 14 S (4. 21%) NMR silent. N has a nuclear moment I = 1 and a sizeable quadrupolar moment that makes the NMR signals usually very broad and dif cult to analyse.
Both an introductory course to broadband dielectric spectroscopy and a monograph describing recent dielectric contributions to current topics, this book is the first to cover the topic and has been hotly awaited by the scientific community.
This second edition of a successful title bridging toxicology and environmental chemistry adopts a unique approach that ‘follows’ chemicals on a molecular level, from the environment through the different uptake mechanisms into the body, to the toxic effect. Along the way, this textbook explains the different routes of degradation and metabolism of the different classes of chemicals, linking general chemical properties to their toxicological equivalents. All the chapters have been thoroughly updated and the contents significantly expanded, including for example new chapters on pesticides, food chemicals and pharmaceuticals, as well as sections discussing endocrine disruptors and carcinogenicity assays. This is an essential text for a wide audience ranging from pharmacologists to environmental chemists and toxicologists.
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.
Nuclear magnetic resonsance (NMR) spectrocopy is the most powerful research tool used in chemistry today, but many chemists have yet to realize its true potential. Recent advances in NMR have led to a formidable array of new techniques - and acronyms - which leaves even the professional spectroscopist bewildered. How, then, can chemists decide which approach will solve their particular structural or mechanistic problem? This book provides a non-mathematical, descriptive approach to modern NMR spectroscopy, taking examples from organic, inorganic, and biological chemistry. It also contains much practical advice about the acquisition and use of spectra. Starting from the simple 'one pulse' sequence, the text employs a 'building block' approach to lead naturally to multiple pulse and two-dimensional NMR. Spectra of readily available compounds illustrate each technique. One- and two- dimensional methods are integrated in three chapters which show how to solve problems by making connections between spins through bonds, through space, or through exchange. There are also chapters on spectrum editing and solids. The final chapter contains a case history which attempts to weave the many strands of the text into a coherent strategy. This second edition reflects the progress made by NMR in the past few years; there is a greater emphasis on inorganic nuclei; some two-colour spectra are used; the treatment of heteronuclear experiments has moved from direct to 'inverse' detection; many new examples and spectra have been included; and the literature to early 1992 has been covered. An accompanying text, Modern NMR spectroscopy: A workbook of chemical problems, by Jeremy Sanders, Edwin Constable, and Brian Hunter, is available from OUP. Using a combination of worked examples and set problems, this workbook provides a practical guide to the accurate interpretation of NMR spectra, which will be of value to students and professional scientists alike.

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