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.

Structure: Nuclear Magnetic Resonance Studies of ThrombinFibrinopeptide and ThrombinHirudin Complexes (F. Ni et al.). ESR and Flourescence Studies of Thrombin Active Site Conformation (L.J. Berliner). Biochemistry: Synthetic Substrates and Inhibitors of Thrombin (J.C. Powers, C.M. Kam). Regulation of Thrombin by Antithrombin and Heparin Cofactor II (S.T. Olson, I. Bjoerk). Hirudin Interactions with Thrombin (S.R. Stone, J.M. Maraganore). Physiology: Functional Domains in Thrombin Outside the Catalytic Site (R. BarShavit et al.). Post Clotting Cellular Effects of Thrombin Mediated by Interaction with HighAffinity Thrombin Receptors (D.H. Carney). Regulation of ThrombinInduced Endothelial Barrier Dysfunction and Prostaglandin Synthesis (J.G.N. Garcia et al.). 3 additional articles. Index.

NMR Methodology for Paramagnetic Proteins; G.N. La Mar, J.S. de Ropp. Nuclear Relaxation in Paramagnetic Metalloproteins; L. Banci. Paramagnetic Relaxation of Water Protons; C.C. Lester, R.G. Bryant. Proton NMR Spectroscopy of Model Hemes; F.A. Walker, U. Simonis. Proton NMR Studies of Selected Paramagnetic Heme Proteins; J.D. Satterlee, et al. Heteronuclear Magnetic Resonance; J. Mispelter, et al. NMR of Polymetallic Systems in Proteins; C. Luchinat, S. Ciurli. Index.

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 applications and the problems and pitfalls encountered in in vivo spectroscopy and imaging.
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 textbook presents in a unified manner the fundamentals of both continuous and discrete versions of the Fourier and Laplace transforms. These transforms play an important role in the analysis of all kinds of physical phenomena. As a link between the various applications of these transforms the authors use the theory of signals and systems, as well as the theory of ordinary and partial differential equations. The book is divided into four major parts: periodic functions and Fourier series, non-periodic functions and the Fourier integral, switched-on signals and the Laplace transform, and finally the discrete versions of these transforms, in particular the Discrete Fourier Transform together with its fast implementation, and the z-transform. This textbook is designed for self-study. It includes many worked examples, together with more than 120 exercises, and will be of great value to undergraduates and graduate students in applied mathematics, electrical engineering, physics and computer science.

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. It is an essential resource for both novices and experts in the field of oxidant and oxidative stress biology.

Electron magnetic resonance spectroscopy is undergoing something akin to a renaissance that is attributable to advances in microwave circuitry and signal processing software. EPR: Instrumental Methods is a textbook that brings the reader up to date on these advances and their role in providing better experimental techniques for biological magnetic resonance. Chapters in this book guide the reader from basic principles of spectrometer design through the advanced methods that are providing new vistas in disciplines such as oximetry, imaging, and structural biology.
Key Features:
Spectrometer design, particularly at low frequencies (below X-band),
Design of spectrometer components unique to ENDOR and ESEEM,
Optimization of EMR spectrometer sensitivity spanning many octaves,
Algorithmic approach to spectral parameterization,
Application of Fourier Methods to polymer conformation, oximetry, and imaging.

In vivo nuclear magnetic and electron spin resonance spectroscopy is concerned, inter alia, with the noninvasive observation of metabolic changes in living systems, including animals and humans. Typically, the physiologi cal (or pathological) state of an organ or tissue is monitored. This multi faceted approach was developed during the 1980s. It is still a research technique, but will undoubtedly become a clinical tool. We are proud to present this volume (the eleventh of our series) in which some of the pioneers in this area summarize their contributions and review related literature. Bolinger and Lenkinski describe a variety of localization methods suitable for clinical applications of NMR spectroscopy. Schleich, Caines, and Rydzewski summarize their contributions to approaches involving off-resonance rotating frame relaxation and critically compare these with other NMR techniques that may yield similar information. 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. Sodium plays an important role in living systems, a key aspect being the large gradient between intra- and extracellular concentrations of sodium that is maintained by a variety of transport mechanisms. Miller and Elgavish give us a comprehensive review of an important research tool in this 23 area- Na NMR spectroscopy as aided by shift reagents."

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. Large Proteins, Complexes, and Membrane Proteins and II. Pulse Methods. Volume 17 contains major advances in: I. Com- tational Methods and II. Structure and Dynamics. The opening chapter of volume 17 starts with a consideration of some important aspects of modeling from spectroscopic and diffraction data by Wilfred van Gunsteren and his colleagues. The next two chapters deal with combined automated assignments and protein structure determination, an area of intense research in many laboratories since the traditional manual methods are often inadequate or laborious in handling large volumes of NMR data on large proteins. First, Werner Braun and his associates describe their experience with the NOAH/DIAMOD protocol developed in their laboratory.

Volume 16 marks the beginning of a special topic series devoted to modern techniques in protein NMR, under the Biological Magnetic Resonance series. This volume is being followed by Volume 17 with the subtitle Structure Computation and Dynamics in Protein NMR. Volumes 16 and 17 present some of the recent, significant advances in biomolecular NMR field with emphasis on developments during the last five years. We are honored to have brought together in these volumes some of the world's foremost experts who have provided broad leadership in advancing this field. Volume 16 contains advances in two broad categories: the first, Large Proteins, Complexes, and Membrane Proteins, and second, Pulse Methods. Volume 17, which will follow covers major advances in Computational Methods, and Structure and Dynamics. In the opening chapter of Volume 16, Marius Clore and Angela Gronenborn give a brief review of NMR strategies including the use of long range restraints in the structure determination of large proteins and protein complexes. In the next two chapters, Lewis Kay and Ron Venters and their collaborators describe state-of-t- art advances in the study of perdeuterated large proteins. They are followed by Stanley Opella and co-workers who present recent developments in the study of membrane proteins. (A related topic dealing with magnetic field induced residual dipolar couplings in proteins will appear in the section on Structure and Dynamics in Volume 17).

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 spectroscopy. The conferences on biological magnetic resonance now have parallel sessions rather than the single, common session of earlier days. Moreover, topical meetings are becoming more frequent. Therefore, this and future volumes of our series will also focus on specific topical areas. We are proud to present Volume 10 of our series. It focuses on Carbohydrates and Nucleic Acids. In an extensive chapter, Kamerling and Vliegenthart use oligosaccharide-alditols released from mucin-type- glycoproteins to illustrate the power of proton NMR spectroscopy in the determination of carbohydrate structure. Wemmer gives a detailed coverage of the arsenal of modern NMR methods now available for structural studies of nucleic acids. Forthcoming volumes will focus on In Vivo Spectroscopy and Protein Structure. As always, we are anxious to get feedback from the readers and hear their comments and suggestions. Lawrence J."

We present here the second issue devoted entirely to the spin-labeling technique as part of Biological Magnetic Resonance. Volume 14 commemorates a modifi- tion in our editorial policy with the retirement of my esteemed coeditor, Jacques Reuben. From thisjuncture into the future, each issue will focus on some special topic in magnetic resonance. Each volume will be organized in most cases by guest editors, for example forthcoming issues will address the following topics: in vivo magnetic resonance (P. Robitaille and L. J. Berliner, eds. ) Modern techniques in proton NMR ofproteins (R. Krishna and L. J. Berliner, eds. ) Instrumental techniques of EPR (C. Bender and L. J. Berliner, eds. ) 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). Someobvious omissions, such as multiquantum EPR and very high-frequency FT-ESR were unfortunately not possible for this volume. Perhaps they will appear in Spin Labeling: 2001. Lastly it is a pleasure to honor two scientists whose contributions were both pioneering and pivotal to the spin label technique: Professor Eduard G. Rozantsev (Moscow), whose synthetic feats in nitroxyl chemistry set the broad stage for a versatile catalog of labels; and Professor Harden M. McConnell, last year's Int- national ESR (EPR) Society Gold Medalist, who conceived and developed the spin label technique to address many biological problems (proteins, enzymes, m- branes, cells, immune response, etc. ). Lawrence J.

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.

Biomedical EPR - Part A focuses on applications of EPR spectroscopy in the areas of free radicals, metals, medicine, and physiology. 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 which lead into up-to-date reviews that provide perspective on the wide range of questions that can be addressed by EPR.

Key Features:
Free Radicals in Medicine

Radicals in vivo and in Model Systems, and their Study by Spin Trapping

In vivo EPR, including Oximetry and Imaging

Time Domain EPR at Radio Frequencies

EPR of Copper Complexes: Motion and Frequency Dependence

Time Domain EPR and Electron Spin Echo Envelope Modulation

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. It is an essential resource for both novices and experts in the field of oxidant and oxidative stress biology.

We take great pleasure in presenting Vol. IV of Biological Magnetic Resonance, a series that continues to give us pride. In this volume, we are pleased to have our first chapter on the applications of ESR to problems in medicine, written by Butterfield. Armitage and Otvos describe their extensive Cd-l13 NMR study in a chapter that should delight the spectroscopists as well as the biochemists, since the systems investigated have not yet been modeled. Kaptein presents an eloquent exposition of the principles and applications to biological systems of the photo-CIDNP technique, to which he has made pioneering contributions. Perkins tells everything one always wanted to know about the applications of ring current calculations in structural studies of biological macromolecules. Our philosophy has been, and continues to be, to present topics of current interest by authors who are active in their field, while maintaining the inter national flavor of the series. Ideally, the coverage of each topic should approach that found both in a textbook and in a reference book, rather than being a mere literature review. We are grateful to the authors for their cooperation in this respect. We continue to solicit the comments and suggestions of our readers and our colleagues, and thank those who have already responded, including the reviewers in the periodicals. Lawrence J. Berliner Jacques Reuben ix Contents Chapter 1 Spin Labeling in Disease D. Allan Butterfield 1. Introduction ...................................... . 2. Membrane Structure . . . . . . . . . . . . . . . . . . . . . . . . . . 2 . . . . . . . 2.1. General Principles. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 2 2.2. The Erythrocyte Membrane. . . . . . . . . . . . . . . . . . . 4 . . . . .

Volume 16 marks the beginning of a special topic series devoted to modern techniques in protein NMR, under the Biological Magnetic Resonance series. This volume is being followed by Volume 17 with the subtitle Structure Computation and Dynamics in Protein NMR. Volumes 16 and 17 present some of the recent, significant advances in biomolecular NMR field with emphasis on developments during the last five years. We are honored to have brought together in these volumes some of the world's foremost experts who have provided broad leadership in advancing this field. Volume 16 contains advances in two broad categories: the first, Large Proteins, Complexes, and Membrane Proteins, and second, Pulse Methods. Volume 17, which will follow covers major advances in Computational Methods, and Structure and Dynamics. In the opening chapter of Volume 16, Marius Clore and Angela Gronenborn give a brief review of NMR strategies including the use of long range restraints in the structure determination of large proteins and protein complexes. In the next two chapters, Lewis Kay and Ron Venters and their collaborators describe state-of-t- art advances in the study of perdeuterated large proteins. They are followed by Stanley Opella and co-workers who present recent developments in the study of membrane proteins. (A related topic dealing with magnetic field induced residual dipolar couplings in proteins will appear in the section on Structure and Dynamics in Volume 17).

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, * Written by the world's foremost experts who have provided broad leadership in advancing the protein NMR field.

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.

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.

We present here the second issue devoted entirely to the spin-labeling technique as part of Biological Magnetic Resonance. Volume 14 commemorates a modifi- tion in our editorial policy with the retirement of my esteemed coeditor, Jacques Reuben. From thisjuncture into the future, each issue will focus on some special topic in magnetic resonance. Each volume will be organized in most cases by guest editors, for example forthcoming issues will address the following topics: in vivo magnetic resonance (P. Robitaille and L. J. Berliner, eds. ) Modern techniques in proton NMR ofproteins (R. Krishna and L. J. Berliner, eds. ) Instrumental techniques of EPR (C. Bender and L. J. Berliner, eds. ) 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). Someobvious omissions, such as multiquantum EPR and very high-frequency FT-ESR were unfortunately not possible for this volume. Perhaps they will appear in Spin Labeling: 2001. Lastly it is a pleasure to honor two scientists whose contributions were both pioneering and pivotal to the spin label technique: Professor Eduard G. Rozantsev (Moscow), whose synthetic feats in nitroxyl chemistry set the broad stage for a versatile catalog of labels; and Professor Harden M. McConnell, last year's Int- national ESR (EPR) Society Gold Medalist, who conceived and developed the spin label technique to address many biological problems (proteins, enzymes, m- branes, cells, immune response, etc. ). Lawrence J.

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. Large Proteins, Complexes, and Membrane Proteins and II. Pulse Methods. Volume 17 contains major advances in: I. Com- tational Methods and II. Structure and Dynamics. The opening chapter of volume 17 starts with a consideration of some important aspects of modeling from spectroscopic and diffraction data by Wilfred van Gunsteren and his colleagues. The next two chapters deal with combined automated assignments and protein structure determination, an area of intense research in many laboratories since the traditional manual methods are often inadequate or laborious in handling large volumes of NMR data on large proteins. First, Werner Braun and his associates describe their experience with the NOAH/DIAMOD protocol developed in their laboratory.

In vivo nuclear magnetic and electron spin resonance spectroscopy is concerned, inter alia, with the noninvasive observation of metabolic changes in living systems, including animals and humans. Typically, the physiologi cal (or pathological) state of an organ or tissue is monitored. This multi faceted approach was developed during the 1980s. It is still a research technique, but will undoubtedly become a clinical tool. We are proud to present this volume (the eleventh of our series) in which some of the pioneers in this area summarize their contributions and review related literature. Bolinger and Lenkinski describe a variety of localization methods suitable for clinical applications of NMR spectroscopy. Schleich, Caines, and Rydzewski summarize their contributions to approaches involving off-resonance rotating frame relaxation and critically compare these with other NMR techniques that may yield similar information. 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. Sodium plays an important role in living systems, a key aspect being the large gradient between intra- and extracellular concentrations of sodium that is maintained by a variety of transport mechanisms. Miller and Elgavish give us a comprehensive review of an important research tool in this 23 area- Na NMR spectroscopy as aided by shift reagents.

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 spectroscopy. The conferences on biological magnetic resonance now have parallel sessions rather than the single, common session of earlier days. Moreover, topical meetings are becoming more frequent. Therefore, this and future volumes of our series will also focus on specific topical areas. We are proud to present Volume 10 of our series. It focuses on Carbohydrates and Nucleic Acids. In an extensive chapter, Kamerling and Vliegenthart use oligosaccharide-alditols released from mucin-type- glycoproteins to illustrate the power of proton NMR spectroscopy in the determination of carbohydrate structure. Wemmer gives a detailed coverage of the arsenal of modern NMR methods now available for structural studies of nucleic acids. Forthcoming volumes will focus on In Vivo Spectroscopy and Protein Structure. As always, we are anxious to get feedback from the readers and hear their comments and suggestions. Lawrence J.

We are pleased to present this second volume of a series that has already received much interest. The application of magnetic resonance methods to the study of actual biological systems as contrasted to cell-free samples, although not entirely novel, as demonstrated by Civan and Shporer in Volume I, has taken on new dimensions with the use of phosphorus-31 and carbon-13 NMR in studying cells, tissues, and organelles. The applications of 31 P NMR to such systems is reviewed in this volume, while carbon-13 will be covered in a later one. The use of nitroxide spin labels has grown to the point where it now may be considered a common biological technique. The synthesis and applications of a new class of nitroxides is described in this volume. ESR spectroscopy of paramagnetic ions is a powerful approach to studying molecular and structural details, as the chapter by Boas, Pilbrow, and Smith on the ESR of copper in Volume 1 has shown. In this volume the ESR of molybdenum and iron is treated in a comparable fashion. 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."