Applications of NMR Spectroscopy


Book Description

Applications of NMR Spectroscopy is a book series devoted to publishing the latest advances in the applications of nuclear magnetic resonance (NMR) spectroscopy in various fields of organic chemistry, biochemistry, health and agriculture. The fifth volume of the series features several reviews focusing on NMR spectroscopic techniques for identifying natural and synthetic compounds (polymer and peptide characterization, GABA in tinnitus affected mice), medical diagnosis and therapy (gliomas) and food analysis. The spectroscopic methods highlighted in this volume include high resolution proton magnetic resonance spectroscopy and solid state NMR.




15N-NMR Spectroscopy


Book Description

After the proton and carbon, nitrogen is, with oxygen, the most impor tant atom in organic and especially bioorganic molecules. However, the development of nitrogen spectroscopy is indeed very recent. This is due to the fact that nitrogen-14, which is the naturally abundant iso tope, suffers, for structural studies, from the disadvantages inherent in nuclei with a quadrupolar moment (Table 1.1). Actually, indirect 15N measurements were reported in the early days of double resonance spectroscopy and the first direct detection of 15N resonance signals at the natural abundance level was realized in 1964 (R 17) at 4.33 MHz 1 (~ 1T) using a 15 mm o.d. cell in the field sweep mode (~ 0.16 min- ). Signal-to-noise ratios only of 3-4 were obtained for neat liquids and this low sensitivity of the 15N resonance still remains the main dis advantage for 15 spectroscopy (Table 1.1). However, nitrogen-15 has, N probably more than any other nucleus, benefited from the advances of NMR technology, i.e. Fourier transformation, multinuclear facilities, wide-bore super conducting solenoids, and, with the new generation of spectrometers, 15N-NMR is entering the field of routine investigation. Nevertheless, in spite of these spectacular improvements, obtaining 15N spectra of diluted species or large biochemical molecules is often not very easy and a good knowledge of the relaxation properties pecu liar to 15N may be necessary in order to adjust the pulse sequences and the decoupler duty cycle correctly (Section 2).




The Multinuclear Approach to NMR Spectroscopy


Book Description

The field of nuclear magnetic resonance has experienced a number of spectacular developments during the last decade. Fourier transform methodology revolutionized signal acquisition capabilities. Superconducting magnets enhanced sensitivity and produced considerable improvement in spectral dispersion. In areas of new applicat ions, the life sciences particularly bene fited from these developments and probably saw the largest increase in usage. NMR imaging promises to offer a noninvasive alternative to X rays. High resolution is now achievable with solids, through magic angle spinning and cross polarization, so that the powers of NMR are applicable to previously intractable materials such as polymers, coal, and other geochemicals. The ease of obtaining relaxation times brought an important fourth variable, after the chemical shift, the coupling constant, and the rate constant, to the examination of structural and kinetic problems i~ all fields. Software development, particularly in the area of pulse sequences, created a host of useful tech niques, including difference decoupling and difference nuclear Overhauser effect spectra, multidimensional displays, signal enhancement (INEPT), coupling constant analysis for connectivity (INADEQUATE), and observation of specific structural classes such as only quaternary carbons. Finally, hardware development gave us access to the entire Periodic Table, to the particular advan tage of the inorganic and organometallic chemist. At the NATO Advanced Study Institute at Stirling, Scotland, the participants endeavored to examine all these advances, except imaging, from a multidisciplinary point of view.




Nitrogen NMR


Book Description

To date nitrogen NMR has been discussed in research papers and review articles throughout the scientific literature. It has been our aim in preparing this book to provide a comprehen sive account of the widely spread applications of nitrogen NMR. The relevant literature has been surveyed from the beginnings of NMR until early 1972. The steady annual growth in the number of references cited since 1965 is ample evidence of the ever increasing importance of the subject. Sufficient theoretical and experimental background is given for an understanding of the applications dealt with in later chapters. The basic principles of NMR are developed with a theoretical approach to chemical shifts and spin-spin coupling constants, particular emphasis being given to nitrogen nuclei. Following this the experimental aspects of nitrogen NMR are adequately described. Special emphasis is given to the observable effects of the nuclear quadrupole moment of the 14 N nucleus. It is appro priate that this topic be dealt with in depth since quadrupolar interactions frequently dominate the information available from a study of the 14 N nucleus and other nuclei spin coupled to it. The applications of nitrogen chemical shift data to organic and inorganic molecules are covered in two extensive chapters which include the effects of paramagnetism on nitrogen NMR.




NMR Spectroscopy


Book Description

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.




Biological NMR Spectroscopy


Book Description

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.




Experimental Approaches of NMR Spectroscopy


Book Description

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.







High-resolution NMR Techniques in Organic Chemistry


Book Description

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.




Fundamentals of Protein NMR Spectroscopy


Book Description

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.