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.

Nuclear Magnetic Resonance offers an accessible introduction to the physical principles of liquid-state NMR, with examples, applications, and exercises provided throughout to enable beginning undergraduates to get to grips with this important analytical technique.

Nuclear magnetic resonance spectroscopy is presently going through an explosive phase of development. This has been brought about largely on account of the advent of Fourier transform NMR spectrometers linked to powerful microcomputers which have opened up a whole new world for structural chemists and biochemists. This is exemplified by a host of publications, especially on new pulse sequences, which continue to provide new exciting modifications for recording two-dimensional NMR. Moreover, NMR is no longer confined to structural chemists but has moved firmly into the area of medicine as a powerful nondestructive body scanning technique. With this background, I felt that there was need for a text which would provide a fairly comprehensive account of the important features of 1 H- and 13C-NMR spectroscopy in one book, as well as make available an up-to-date account of recent developments of new pulse sequences, with particular reference to 2D-NMR spectroscopy. Since this book is written for students of chemistry and biochemistry as well as for biology students who have chemistry as a subsidiary, it was decided to avoid a complex mathematical treatment and to present, as far as possible without oversimplification, a qualitative account of 1 H- and 13C-NMR spectroscopy as it is today. I hope that the book satisfactorily meets these objectives.

Nuclear Magnetic Resonance in Biochemistry: Principles and Applications focuses on the principles and applications of nuclear magnetic resonance (NMR) in biochemistry. Topics covered include experimental methods in NMR; the mechanisms of NMR relaxation; chemical and paramagnetic shifts; spin-spin splitting; the use of NMR in investigations of biopolymers and biomolecular interactions; and molecular dynamics in biological and biochemical systems. This text is comprised of eight chapters; the first of which gives an overview of NMR spectroscopy and its use in studies of biological systems. The next two chapters discuss the theoretical basis for NMR applications in biochemistry, with emphasis on Bloch equations, quantum mechanics, correlation function and correlation time, double resonance, and chemical exchange. The reader is then introduced to the basis for chemical shifts and spin-spin splitting, along with several examples of the use of these NMR parameters in studies of small molecule interactions and structure. The experimental apparatus and procedures employed in NMR studies, Fourier transform NMR, and NMR spectral parameters of small molecules interacting with macromolecules are also considered. The book highlights the information obtainable from the spectra of biopolymers, and then concludes with a chapter on NMR investigations of the state of motion of lipids in membranes and model membranes; water in macromolecular and cellular systems; and sodium ion in biological tissue. This book is intended primarily for chemists, biochemists, biophysicists, and molecular biologists, as well as graduate students.

The revolutionary impetus of the NMR methods in organic chemistry has parallels in the field of boron chemistry. lIB NMR spectroscopy provided a basis for the elucida tion of structures and reactions of the boron hydrides. However, although many studies have been carried out with the higher boranes, carboranes, metalloboranes, etc. , and although certain patterns have emerged, the correlation between the observed chemical shift and the assigned structural unit is still not fully understood. Therefore, predictions in this area are still rather limited, and semiquantitative interpretations are not yet pos sible. Several years ago Eaton and Lipscomb sUpImarized the status in this field in their book "NMR Studies of Boron Hydrides and Related Compounds" and a plethora of new data has accumulated since then. The book also contained material on simple bo rane derivatives, but they were not discussed in any detail. On the other hand many systematic studies, both synthetic and spectroscopic, have been conducted on these simple boron materials in the last decade. Thus a large amount of NMR information is available, not only on lIB but also on 1 H, 1 3 C, and 14 N. However, this information is widely scattered in the literature, and often the data are not discussed at all. It see med appropriate, therefore, to collect these data and to present them in one volume.

Nine chapters cover: fundamental principles; experimental methods; the chemical shift; coupling of nuclear spins; nuclear relaxation and chemical rate processes; two-dimensional nuclear magnetic resonance spectroscopy; macromolecules; NMR of solids; special topics. Annotation copyrighted by Book News, Inc., Portland, OR

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.