Bücher der Reihe Biological Magnetic Resonance

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 examples of how experimental data is worked up to produce a distance estimate, and realistic assessments of uncertainties and of the range of applicability, along with examples of the power of the technique to answer biological problems. The first chapter is an overview, by two of the editors, of EPR methods to determine distances, with a focus on the range of applicability. The next chapter, also by the Batons, reviews what is known about electron spin relaxation times that are needed in estimating distances between spins or in selecting appropriate temperatures for particular experiments. Albert Beth and Eric Hustedt describe the information about spin-spin interaction that one can obtain by simulating CW EPR line shapes of nitroxyl radicals. The information in fluid solution CW EPR spectra of dual-spin labeled proteins is illustrated by Hassane Mchaourab and Eduardo Perozo.

While we still intend to produce a volume only if a suitable number of excellent chapters in the forefront of biological magnetic resonance are available, our philosophy is to present a pedagogical yet critical description and review of selected topics in mag netic resonance of current interest to the community of biomedical scien tists.

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.

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.

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

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.

Albert Beth and Bruce Robinson have contributed a detailed chapter on the analysis of these labels in the slow-motion regime while Jane Park and Wolfgang Trommer present the advantages for specific biochemical examples in our "applications" section.

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.

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.

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.

It covers a broad spectrum of topics, including the history of fMRI's development using endogenous MR blood contrast, neurovascular coupling, pulse sequences for fMRI, quantitative fMRI;

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.

The foundation for understanding the function and dynamics of biological systems is not only knowledge of their structure, but the new methodologies and applications used to determine that structure. This volume in Biological Magnetic Resonance emphasizes the methods that involve Ultra High Field Magnetic Resonance Imaging.

Starting from a comprehensive quantum mechanical description, this book introduces the optical (IR, Raman, UV/Vis, CD, fluorescence and laser spectroscopy) and magnetic resonance (1D and 2D-NMR, ESR) techniques.

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

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.

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.

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.

This book describes the methods of analysis and determination of oxidants and oxidative stress in biological systems. Reviews and protocols on select methods of analysis of ROS, RNS, oxygen, redox status, and oxidative stress in biological systems are described in detail.

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.

a

) 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).

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.