We are pleased to present Volume 9 of our highly successful series, which now celebrates 12 years of providing the magnetic resonance community with topical, authoritative chapters on new aspects of biological magnetic resonance. As always, we try to present a diversity of topic coverage in each volume, ranging from applications of in vivo magnetic resonance to more fundamental aspects of electron spin resonance and nuclear magnetic resonance. Philip Yeagle presents an eagerly awaited chapter on 31p NMR studies of membranes and membrane protein interactions. Alan Marshall has con- tributed...

Distance measurements in biological systems by EPR The foundation for understanding function and dynamics of biological systems is knowledge of their structure. Many experimental methodologies are used for determination of structure, each with special utility. Volumes in this series on Biological Magnetic Resonance emphasize the methods that involve magnetic resonance. This volume seeks to provide a critical evaluation of EPR methods for determining the distances between two unpaired electrons. The editors invited the authors to make this a very practical book, with specific numerical...

The first of a two volume set, Volume 12 provides a long-awaited compilation of NMR theory to paramagnetic molecules. International experts report the latest developments in NMR methodology as applied to strongly relaxed and shifted resonances, detail the theoretical aspects of paramagnetic shift and relaxation, and discuss the interpretive bases of these molecular properties in relation to the structure and function of various paramagnetic molecules.

Research on thrombin structure and function has progressed significantly over the past three decades. We are continually discovering new functions f()r this enzyme in biology. Yet, until quite recently, a full, detailed, three- dimensional picture of its structure was difficult to attain. We believe that this text represents a turning point and, more appropriately, a new start- ing point for thrombin studies. Our goal for this text is to present a thorough and rounded-out coverage of thrombin chemistry and biochem- istry in order to provide the biochemist and physiologist with an excellent...

In Vivo EPR (ESR) is a textbook on this relatively new subject in biomedical electron spin resonance. While a few chapters have appeared in special topics volumes in this series, this book covers the principles and theory, instrumentation as well as the latest applications at the time of its writing. The authors are world-renowned experts and pioneers in their fields. This book is divided into two major sections dealing with theory and instrumentation, and aspects of biochemistry, in vitro and in vivo applications. A significant amount of detail is devoted to clinical...

We present this special topics volume on an area which has not received thorough coverage for over 12 years. Spin Labeling: Theory and Applications represents a complete update on new theoretical aspects and applications of the spin-label method. In the "line-shape theory" sections, we are especially pleased to include an IBM-compatible diskette supplied by David Schneider and Jack Freed which contains fast, accurate, ready-to-use software for slow-motion simulations. Barney Bales discusses inhomogeneous broadening phenomena in detail. Several developments in techniques and interpretation in...

Volume 17 is the second in a special topic series devoted to modern techniques in protein NMR, under the Biological Magnetic Resonance series. Volume 16, with the subtitle Modern Techniques in Protein NMR, is the first in this series. These two volumes present some of the recent, significant advances in the biomolecular NMR field with emphasis on developments during the last five years. We are honored to have brought together in these volume some of the world s foremost experts who have provided broad leadership in advancing this field. Volume 16 contains - vances in two broad categories: I....

This volume constitutes a compilation of the latest experiments and theories on a rapidly evolving and maturing field in MRI/MRS, which is the use of the stable isotope 13-C. The 13-C is used to probe the chemistry, mechanism, and function in living systems.
All the chapters are written by experts in the field who discuss topics such as Tracer Theory and the Suitability of 13-C NMR', Applications of 13-C to Studies of Human Brain Metabolism', etc.

In the past ten years or so, biological magnetic resonance (NMR and ESR) has fully blossomed and become highly branched. In the 1970s and earlier, a practitioner in biological magnetic resonance was using virtually all of the available methods suitable for his research, with the latter covering a diverse range of systems. Today, the focus of an individual laboratory is actually much narrower, with respect to both the methods and the systems investigated. Thus, those who investigate protein structure by multi- dimensional NMR spectroscopy do not usually engage in studies involving in vivo...

Protein NMR for the Millennium is the third volume in a special thematic series devoted to the latest developments in protein NMR under the Biological Magnetic Resonance umbrella. This book is divided into three major sections dealing with significant recent advances in the study of large proteins in solution and solid state, structure refinement, and screening of bioactive ligands.
Key Features:

• TROSY,
• Segmental isotope labeling of proteins,
• Hydrogen bond scalar couplings,
• Structure refinement based on residual dipolar couplings,...