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Biological Magnetic Resonance : Biological Magnetic Resonance - Lawrence Berliner

Biological Magnetic Resonance

Biological Magnetic Resonance

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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. The first chapters, as always, address a subject related to in-vivo biology. Gabby Elgavish addresses NMR spectroscopy of the intact heart. lain Campbell and colleagues present a state-of-the-art description of NMR methods for probing enzyme kinetics in intact cells and tissues. Klaus Mobius and Wolfgang Lubitz have produced a thorough review of the principles and applications of ENDOR spectroscopy in photobiology and biochemistry including discussions of liquid and solid state ENDOR as well as CIDEP-enhanced ENDOR. The final chapter by Hans Vogel and Sture Forsen addresses a contemporary problem in inorganic biochemistry, namely cation binding to calcium binding proteins. We are pleased to announce that a special forthcoming volume will be devoted entirely to the subject of "Spin Labeling: Theory and Applications (3rd compendium)." A substantial degree of progress has occurred in this important area of ESR in biology since the last treatise on the subject in 1979. Lastly, we acknowledge our colleagues in the field who continue to support this excellent series both as subscribers and contributors. We pledge to continue servicing the community as long as the need exists.

An excellent collection of review articles ... A significant compilation of the theoretical basis of emerging technologies and a summary of their successes.' Journal of the American Chemical Society The reviews presented are diverse in nature ... continue to provide fresh analysis of the latest science ... succeed in being comprehensive in the subject areas.' Trends in Analytical Chemistry

1 NMR Spectroscopy of the Intact Heart.- 1. Introduction.- 2. Experimental Methods.- 2.1. The Perfused Heart.- 2.2. NMR Parameters.- 2.2.1. The Intensity of 31P NMR Signals.- 2.2.2. Changes in Chemical Shifts.- 2.2.3. Saturation Transfer.- 2.3. Methods of Inducing Perturbations in the Perfused Heart.- 3. Applications.- 3.1. Hypoxia.- 3.2. Ischemia.- 3.3. Myocardial Protection.- 3.4. Myocardial Creatine Kinase.- 3.5. Chemical Perturbations.- 3.6. Cardiac Cycle.- 3.7. Respiration.- 3.8. Cardiac Metabolism.- 3.9. In Vivo Detection.- 4. Concluding Remarks.- References.- 2 NMR Methods for Studying Enzyme Kinetics in Cells and Tissue.- 1. Introduction.- 2. Metabolic Pathways.- 3. Measurements of Concentration Changes.- 4. Line Shape, T2 and T1.- 5. Magnetization Transfer.- 5.1. Experimental Methods.- 5.2. Effect of the Equilibrium Constant on Measurements of Exchange.- 5.3. Exchange Pathway.- 5.3.1. Exchange in a Multienzyme System.- 5.3.2. Exchange Catalyzed by a Single Enzyme.- 6. Isotope Exchange.- 6.1. Detection of Isotope Labels by NMR.- 6.2. The Application of Isotopic Labeling in Studies of Enzymes.- 7. Conclusion.- References.- 3 Endor Spectroscopy in Photobiology and Biochemistry.- 1. Introduction.- 2. Principles of Electron-Nuclear Multiple Resonance Spectroscopy.- 2.1. ENDOR in Liquid Solution.- 2.2. TRIPLE Resonance as an Extension of ENDOR in Solution.- 2.3. Experimental Arrangements.- 2.4. Relaxation Theory of ENDOR/TRIPLE in Solution.- 2.5. ENDOR in Liquid Crystals.- 2.6. CIDEP-Enhanced ENDOR.- 2.6.1. Basic Principles.- 2.6.2. CIDEP-Enhanced ENDOR Detection Strategy: Net Effect versus Multiplet Effect.- 2.6.3. Applications of CIDEP-Enhanced ENDOR.- 2.7. ENDOR in Frozen Solution.- 2.7.1. Local ENDOR.- 2.7.2. Matrix ENDOR.- 2.7.3. Distant ENDOR.- 2.8. Electron Spin-Echo ENDOR and Electron Spin-Echo Modulation Spectroscopy.- 3. Representative Examples.- 3.1. Primary Products of Photosynthesis.- 3.1.1. General Remarks.- 3.1.2. Primary Donors in Bacterial Photosynthesis.- 3.1.3. Electron Acceptors in Bacterial Photosynthesis.- 3.1.4. Primary Donors in Plant Photosynthesis.- 3.1.5. Electron Acceptors in Plant Photosynthesis.- 3.2. Hemes and Hemoproteins.- 3.2.1. General Remarks.- 3.2.2. Hemoglobin and Myoglobin.- 3.2.3. Cytochromes.- 3.2.4. Peroxidases.- 3.3. Metalloproteins.- 3.3.1. Copper Proteins.- 3.3.2. Iron-Sulfur Proteins.- 3.3.3. Other Metals in Enzymatic Systems.- 3.4. Flavins and Flavoproteins.- 3.4.1. General Remarks.- 3.4.2. Flavosemiquinone Model Systems.- 3.4.3. Flavosemiquinones in Enzymatic Systems.- 3.5. Other Biologically Active Organic Species.- 3.5.1. Vitamin Quinones.- 3.5.2. Catechols and Catecholamins.- 3.5.3. Phenothiazines.- 4. Summary.- Recent Developments.- References.- 4 NMR Studies of Calcium-Binding Proteins.- 1. Introduction.- 1.1. Calcium Metabolism.- 1.2. Calcium-Binding Proteins.- 1.3. Choice of Suitable NMR Nuclei.- 2. Calcium-43 NMR Studies.- 2.1. Fast Exchange Conditions.- 2.2. Slow Exchange Conditions.- 3. Magnesium-25 NMR Studies.- 4. Cadmium-113 NMR Studies.- 5. Metal Ion Competition Experiments.- 6. Ligand Interactions.- 7. Proton NMR Studies.- 8. Epilogue.- References.

ISBN: 9780306424557
ISBN-10: 030642455X
Series: Biological Magnetic Resonance : Book 7
Audience: Professional
Format: Hardcover
Language: English
Number Of Pages: 314
Published: 1987
Country of Publication: US
Dimensions (cm): 22.23 x 15.24  x 2.54
Weight (kg): 0.61