Bøger i Biological Magnetic Resonance serien

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.

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.

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.

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.

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.

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.

It explores a broad spectrum of topics including quantum computing, information processing, quantum effects in electron-nuclear coupled molecular spin systems, adiabatic quantum computing, heat bath algorithmic cooling with spins, and gateway schemes of quantum control for spin networks to NMR quantum information.

This book covers the latest developments in metalloenzymes, including characterizing metal bridging in proteins and peptides, copper(II) complexes of marine peptides, high-spin Co(II) in model and metalloprotein systems to enzymes such as the molybdenum-containing enzymes, CW and pulse EPR of cytochrome P450 enzymes and the radical S-adenosylmethionine FeS family. In the previous two related volumes in the Biological Magnetic Resonance series, High-Resolution EPR: Applications to Metalloenzymes and Metals in Medicine and Metals in Biology:Applications of High-Resolution EPR to Metalloenzymes, topics covered included high-resolution EPR methods, iron proteins, nickel and copper enzymes, metals in medicine, iron-sulfur cluster-containing proteins, and molybdenum enzymes. In this volume, new developments in these areas are covered in detail and new areas that have emerged are also detailed. This is an ideal book for graduate students and researchers working in the fields of high-resolution EPR, metalloenzymes, and metals in biology.

This book covers the latest developments in metalloenzymes, including characterizing metal bridging in proteins and peptides, copper(II) complexes of marine peptides, high-spin Co(II) in model and metalloprotein systems to enzymes such as the molybdenum-containing enzymes, CW and pulse EPR of cytochrome P450 enzymes and the radical S-adenosylmethionine FeS family. In the previous two related volumes in the Biological Magnetic Resonance series, High-Resolution EPR: Applications to Metalloenzymes and Metals in Medicine and Metals in Biology:Applications of High-Resolution EPR to Metalloenzymes, topics covered included high-resolution EPR methods, iron proteins, nickel and copper enzymes, metals in medicine, iron¿sulfur cluster-containing proteins, and molybdenum enzymes. In this volume, new developments in these areas are covered in detail and new areas that have emerged are also detailed. This is an ideal book for graduate students and researchers working in the fields of high-resolution EPR, metalloenzymes, and metals in biology.

It explores a broad spectrum of topics including quantum computing, information processing, quantum effects in electron-nuclear coupled molecular spin systems, adiabatic quantum computing, heat bath algorithmic cooling with spins, and gateway schemes of quantum control for spin networks to NMR quantum information.

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;

We are proud to present Volume 3 of Biological Magnetic Resonance, a series that has met with praise from the scientific community. This volume covers the new applications of various multiple irradia­ tion techniques to the NMR of biomolecules; the chapter of Keller and Wuthrich describes much of the technique and its applications to hemo­ proteins. The ESR of some hemoproteins in the single crystal is described by Chien and Dickinson, who also include discussions of techniques and methods for single-crystal ESR of paramagnetically intrinsic and spin­ labeled protein crystals. Mims and Peisach describe the latest applications and results in electron spin echo spectroscopy of several metalloproteins. Two ESR spin probe techniques are reviewed. Chasteen describes the methods and applications of vanadyl(JV) to several systems. Ohnishi and Tokutomi describe studies of phase separations in mixed and model mem­ branes by the nitroxide spin probe technique. We have been successful in continuing to provide topics that are timely and experimentally informative with a heavy emphasis on biolo­ gically relevant applications. We thank our colleagues in the scientific com­ munity for their suggestions on future coverage-we will remain receptive to future suggestions and comments on this series. A tentative topic list for forthcoming volumes is given on the following pages.

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.

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.

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;

Protein NMR. Modern Techniques and Biomedical Applications.

) 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).

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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.

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.

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

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.

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.

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

Published as a companion to Volume 12, the current volume presents the latest advances in electron paramagnetic resonance of iron proteins, metalloproteins, and free radicals. The book features a diskette containing programs for iron ERP spectral simulation and ENDOR analyses.

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.