Nuclear magnetic resonance (NMR) is a physical phenomenon in which nuclei in magnetic field absorb and re-emit electromagnetic radiation. This energy is at a specific resonance frequency which depends on the strength of the magnetic field and the magnetic properties of the isotope of the atoms; in practical applications the frequency is similar to VHF and UHF television broadcasts (60–1000 MHz).
J.W. Akitt and B.E. Mann
Keeping mathematics to a minimum, this book introduces nuclear properties, nuclear screening, chemical shift, spin-spin coupling, and relaxation. It is one of the few books that provides the student with the physical background to NMR spectroscopy from the point of view of the whole of the periodic table rather than concentrating on the narrow applications of 1H and 13C NMR spectroscopy. Aids to structure determination, such as decoupling, the nuclear Overhauser effect, INEPT, DEPT, and special editing, and two dimensional NMR spectroscopy are discussed in detail with examples, including the complete assignment of the 1H and 13C NMR spectra of D-amygdain.
The authors examine the requirements of a modern spectrometer and the effects of pulses and discuss the effects of dynamic processes as a function of temperature or pressure on NMR spectra. The book concludes with chapters on some of the applications of NMR spectroscopy to medical and non-medical imaging techniques and solid state chemistry of both I = F1/2 and I > F1/2 nuclei. Examples and problems, mainly from the recent inorganic/organometallic chemistry literature support the text throughout. Brief answers to all the problems are provided in the text with full answers at the end of the book.
NMR Primer: An HSQC-Based Approach has one aim: to explain the key two-dimensional protein NMR experiment, the 1H,15N-HSQC, along with variants and extensions, in a generally accessible manner. Vector diagrams of one-, two- and three-dimensional pulse sequences are provided, along with accompanying animated versions.
Edited: A Ramamoorthy
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.
Harald Guenther-3rd Edition
Nuclear magnetic resonance (NMR) spectroscopy is one of the most powerful and widely used techniques in chemical research for investigating structures and dynamics of molecules. Advanced methods can even be utilized for structure determinations of biopolymers, for example proteins or nucleic acids. NMR is also used in medicine for magnetic resonance imaging (MRI). The method is based on spectral lines of different atomic nuclei that are excited when a strong magnetic field and a radiofrequency transmitter are applied. The method is very sensitive to the features of molecular structure because also the neighboring atoms influence the signals from individual nuclei and this is
important for determining the 3D–structure of molecules.
This new edition of the popular classic has a clear style and a highly practical, mostly non–mathematical approach. Many examples are taken from organic and organometallic chemistry, making this book an invaluable guide to undergraduate and graduate students of organic chemistry, biochemistry, spectroscopy or physical chemistry, and to researchers using this well–established and extremely important technique. Problems and solutions are included.
Peter Bigler-2nd Edition
Leading software designers and teachers of spectroscopy have pooled their expertise to devise a new series "Spectroscopic Techniques: An Interactive Course". User are able to gain a better understanding of a variety of spectroscopic techniques in these step–by–step guides.