Lawrence Berliner – författare
Biomedical EPR - Part B: Methodology, Instrumentation, and Dynamics
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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
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Computational and Instrumental Methods in EPR
1 091 kr
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2 241 kr
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1 367 kr
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2 822 kr
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Spectroscopic methods are not only important as an analytical tool, they also provide information about fundamental physical and chemical properties of molecules, the molecular and electronic structure, and the dynamic behaviour of molecules. Starting from a comprehensive quantum mechanical description, ESR Spectroscopy in Membrane Biophysics introduces the optical (IR, Raman, UV/Vis, CD, fluorescence and laser spectroscopy) and magnetic resonance (1D and 2D-NMR, ESR) techniques.
ESR Spectroscopy in Membrane Biophysics is a timely review of the increasing interest in using spin-label ESR as an alternative structural technique for NMR or X-ray diffraction. It is aimed at training an audience to learn ESR spectroscopy to determine membrane protein structures, conformational dynamics and protein-lipid interaction.
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Metalloproteins comprise approximately 30% of all known proteins, and are involved in a variety of biologically important processes, including oxygen transport, biosynthesis, electron transfer, biodegradation, drug metabolism, proteolysis, and hydrolysis of amides and esters, environmental sulfur and nitrogen cycles, and disease mechanisms. EPR spectroscopy has an important role in not only the geometric structural characterization of the redox cofactors in metalloproteins but also their electronic structure, as this is crucial for their reactivity. The advent of x-ray crystallographic snapshots of the active site redox cofactors in metalloenzymes in conjunction with high-resolution EPR spectroscopy has provided detailed structural insights into their catalytic mechanisms.
This volume was conceived in 2005 at the Rocky Mountain Conference on Analytical Chemistry (EPR Symposium) to highlight the importance of high-resolution EPR spectroscopy to the structural (geometric and electronic) characterization of redox active cofactors in metalloproteins. We have been fortunate to have enlisted internationally recognized experts in this joint venture to provide the scientific community with an overview of high-resolution EPR and its application to metals in biology. This volume, High-Resolution EPR: Applications to Metalloenzymes and Metals in Medicine, covers high-resolution EPR methods, iron proteins, nickel and copper enzymes, and metals in medicine. An eloquent synopsis of each chapter is provided by John Pilbrow in the Introduction. A second volume, Metals in Biology: Applications of High-Resolution EPR to Metalloenzymes, will appear later this year covering the complement of other metalloproteins.
One of the pioneers in the development of pulsed EPR and its application to metalloproteins was Arthur Schweiger, whose contribution we include in this volume. Unfortunately, he passed away suddenly during the preparation of this volume. The editors andcoauthors are extremely honored to dedicate this volume to the memory of Arthur Schweiger in recognition of his technical advances and insights into pulsed EPR and its application to metalloproteins. Arthur was extremely humble and treated everyone with equal respect. He was a gifted educator with an ability to explain complex phenomena in terms of simple intuitive pictures, had a delightful personality, and continues to be sadly missed by the community.
It is an honor for the editors to facilitate the dissemination of these excellent contributions to the scientific community. Suggestions for future volumes are always appreciated.
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Metal ions in biology is an ever expanding area in science and medicine involving metal ions in proteins and enzymes, their biosynthesis, catalysis, electron transfer, metal ion trafficking, gene regulation and disease. While X-ray crystallography has provided snapshots of the geometric structures of the active site redox cofactors in these proteins, the application of high resolution EPR spectroscopy in conjunction with quantum chemistry calculations has enabled, in many cases, a detailed understanding of a metalloenzymes mechanism through investigations of the geometric and electronic structure of the resting, enzyme-substrate intermediates and product complexes.
This volume, Part II of a two-volume set demonstrates the application of high resolution EPR spectroscopy in determining the geometric and electronic structure of active site metal ion centers in iron sulfur cluster containing metalloproteins, mononuclear molybdenum metalloenzymes, manganese-containing enzymes and novel metalloproteins.
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Computational and Instrumental Methods in EPR
1 091 kr
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549 kr
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687 kr
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687 kr
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Biological Magnetic Resonance
549 kr
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687 kr
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549 kr
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687 kr
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Biological Magnetic Resonance
Volume 6
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Ultra High Field Magnetic Resonance Imaging
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ESR Spectroscopy in Membrane Biophysics
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fMRI: From Nuclear Spins to Brain Functions
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Protein NMR
Modern Techniques and Biomedical Applications
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1 408 kr
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This book covers new techniques in protein NMR, from basic principles to state-of-the-art research. It covers a spectrum of topics ranging from a “toolbox” for how sequence-specific resonance assignments can be obtained using a suite of 2D and 3D NMR experiments and tips on how overlap problems can be overcome. Further topics include the novel applications of Overhauser dynamic nuclear polarization methods (DNP), assessing protein structure, and aspects of solid-state NMR of macroscopically aligned membrane proteins.
This book is an ideal resource for students and researchers in the fields of biochemistry, chemistry, and pharmacology and NMR physics. Comprehensive and intuitively structured, this book examines protein NMR and new novel applications that include the latest technological advances.
This book also has the features of:
• A selection of various applications and cutting-edge advances, such as novel applications of Overhauser dynamic nuclear polarization methods (DNP) and a suite of 2D and 3D NMR experiments and tips on how overlap problems can be overcome
• A pedagogical approach to the methodology
• Engaging the reader and student with a clear, yet critical presentation of the applications
Protein NMR
Modern Techniques and Biomedical Applications
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fMRI: From Nuclear Spins to Brain Functions
2 464 kr
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High Resolution EPR
Applications to Metalloenzymes and Metals in Medicine
2 241 kr
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