Bøger i Biological Magnetic Resonance serien

The field of Very High Frequency EPR (VHF EPR) or sometimes called Very High Field EPR (conveniently, also abbreviated as VHF EPR) has blossomed during the past decade, especially after the original pioneering work of Ya.

Volume 16 marks the beginning of a special topic series devoted to modern techniques in protein NMR, under the Biological Magnetic Resonance series.

Biomedical EPR ¿ Part B focuses on applications of EPR techniques and instrumentation, with applications to dynamics. The book celebrates the 70th birthday of Prof. James S. Hyde, Medical College of Wisconsin, and his contributions to this field. Chapters are written to provide introductory material for new-comers to the field that lead into up-to-date reviews that provide perspective on the wide range of questions that can be addressed by EPR. Key Features:EPR Techniques including Saturation Recovery, ENDOR, ELDOR, and Saturation Transfer Instrumentation Innovations including Loop Gap Resonators, Rapid Mixing, and Time Locked Sub-Sampling Motion in Biological Membranes Applications to Structure Determination in Proteins Discussion of Trends in EPR Technology and Prognosis for the Future About the Editors:Prof. Sandra S. Eaton is John Evans Professor in the Department of Chemistry and Biochemistry at the University of Denver. Her research interests include distance measurements in proteins, EPR of metal ions in biological systems, electron spin relaxation times, and EPR instrumentation. The Eatons co-organize an annual EPR Symposium in Denver. Prof. Gareth R. Eaton is John Evans Professor in the Department of Chemistry and Biochemistry at the University of Denver. His research interests include EPR instrumentation, distance measurements in proteins, EPR of metal ions in biological systems, and electron spin relaxation times.Dr. Lawrence J. Berliner is currently Professor and Chair of the Department of Chemistry and Biochemistry at the University of Denver after retiring from Ohio State University, where he spent a 32-year career in the area of biological magnetic resonance (EPR and NMR). He is the Series Editor for Biological Magnetic Resonance, which he launched in 1979.

Distance measurements in biological systems by EPR The foundation for understanding function and dynamics of biological systems is knowledge of their structure.

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.

Judging from the articles published in Biochemistry, magnetic resonance techniques (NMR and ESR) are now among the most popular methods in biochemical research.

In the first volume some aspects of 1 H NMR spectroscopy of certain classes of In this volume the high-resolu biological macromolecules were discussed.* tion multinuclear NMR spectra of peptides, including the physiologically significant peptide hormones, are reviewed.

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) Thecurrent volume, Spin Labeling: The NextMillennium, presents an excellent collection of techniques and applications that evolved during the past decade since the last volume, volume 8 (1989).

Computational and Instrumental Methods in EPR is devoted to both instrumentation and computation aspects of EPR, while addressing applications such as spin relaxation time measurements.

Key Features: -History of In Vivo EPR, -Principles of Imaging-Theory and Instrumentation, -Time-domain Radio Frequency EPR Imaging, -The Measurement of Oxygen In Vivo Using In Vivo EPR Techniques, -Potential Medical (Clinical) Applications of EPR, -Combining NMR and EPR/ESR for In Vivo Experiments.

This volume was conceived in 2005 at the Rocky Mountain Conference on Analytical Chemistry (EPR Symposium). It highlights the importance of high-resolution EPR spectroscopy to the structural characterization of redox active cofactors in metalloproteins.

We are again proud to present an excellent volume of contemporary topics in NMR and EPR to the biological community. The philosophy behind the volume and the presentation of each chapter remains at the high level reflected in our earlier volumes: to be current, pedagogical, and critical.

Key Features: TROSY, Segmental isotope labeling of proteins, Hydrogen bond scalar couplings, Structure refinement based on residual dipolar couplings, Written by the world's foremost experts who have provided broad leadership in advancing the protein NMR field.

This volume was conceived in 2005 at the Rocky Mountain Conference on Analytical Chemistry (EPR Symposium). It highlights the importance of high-resolution EPR spectroscopy to the structural characterization of redox active cofactors in metalloproteins.

Focuses on applications of EPR spectroscopy in the areas of free radicals, metals, medicine, and physiology. This book celebrates the 70th birthday of Prof. James S Hyde, Medical College of Wisconsin, and his contributions to this field.

Electron magnetic resonance spectroscopy is undergoing something akin to a renaissance that is attributable to advances in microwave circuitry and signal processing software. This textbook talks about these advances and their role in providing better experimental techniques for biological magnetic resonance.

Focuses on applications of EPR techniques and instrumentation, with applications to dynamics. This work covers such topics as: EPR techniques including Saturation Recovery, ENDOR, ELDOR, and Saturation; Transfer instrumentation innovations, including loop gap resonators, rapid mixing, and time locked sub-sampling motion in biological membranes.

Volume 17 is the second in a special topic series devoted to modern techniques in protein NMR, under the Biological Magnetic Resonance series.

Chang and James outline their approach and share their experience with the technical aspects 1 31 of H and P NMR spectroscopy and spatially localized spectroscopy in studies of brain ischemia.

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.

In the past ten years or so, biological magnetic resonance (NMR and ESR) has fully blossomed and become highly branched. Thus, those who investigate protein structure by multi dimensional NMR spectroscopy do not usually engage in studies involving in vivo spectroscopy.

Computational and Instrumental Methods in EPR is devoted to both instrumentation and computation aspects of EPR, while addressing applications such as spin relaxation time measurements.