Biological magnetic resonance

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書誌事項

Biological magnetic resonance

edited by Lawrence J. Berliner and Jacques Reuben

Springer, c1978

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注記

Reprint. Originally published: New York : Springer , c1978

Printed in Japan

Includes bibliographical references and index

内容説明・目次

内容説明

Biological magnetic resonance (NMR and EPR) is a rapidly expanding area of research with much activity in most universities and research institutions. International conferences are held biennially with an increasing number of participants. With the introduction of sophisticated and continuously im proving instrumentation, biological magnetic resonance is approaching the state of a common physical method in biochemical, biomedical, and bio logical research. The lack of monograpbs on the subject had been con spicuous for a long time. This gap started to close only recently. However, because of the rapid expansion and intensive research, many texts are dated by the time of their appearance. Therefore we have undertaken the editing of a series that is intended to provide the practicing chemist, biochemist, or biologist with the advances and progress in selected contemporary topics. In seeking to make the series as authoritative as possible, we have invited authors who have not only made significant contributions but who are also currently active in their fields. We hope that their expertise as well as their first hand experience as reflected in the chapters of this volume will be of benefit to the reader, inter alia, in planning his own experiments and in critically evaluating the current literature.

目次

1 NMR of Sodium-23 and Potassium-39 in Biological Systems.- 1. Introduction.- 2. Theoretical Background.- 3. Relaxation Rates in Simple Aqueous Solution.- 4. Effects of Complexing Agents and Ionophores.- 5. Electrostatic Interactions and Effects of Polyelectrolytes.- 6. Spectra in Ordered Systems.- 7. Measurements in Biological Tissues.- References.- 2 High-Resolution NMR Studies of Histones.- 1. Introduction.- 2. Studies of the Self-Aggregation of the "Core Histones" Using Proton Spectroscopy.- 2.1. Histone H2B.- 2.2. Histone H2A.- 2.3. Histone H4.- 2.4. Histone H3.- 3. Carbon-13 Studies of Histone Self-Aggregation.- 4. Summary of Histone Self-Aggregation Studies.- 5. Interactions of Single Histones with DNA.- 6. Histone Complexes.- 6.1. The Arginine-Rich Tetramer (H3/H4)2.- 6.2. Peptide Studies of the H3/H4 Complex.- 6.3. The Moderately Lysine-Rich Complex (H2A/H2B)1.- 7. The Lysine-Rich Histone H1.- 7.1. The Globular Segment of H1.- 7.2. Phosphorylated H1.- 8. The Lysine-Rich Histone H5 from Nucleated Erythrocytes.- 8.1. The Globular Segment of H5.- 8.2. Denaturation/Renaturation Studies of H5.- 9. Marine Invertebrate Sperm H1s ((?1s).- 10. Nonhistone Chromosomal Proteins.- 11. Histone H1 Interactions in Chromatin.- 11.1. Chromatin.- 11.2. H1-DNA.- 11.3. Marine Invertebrate Sperm H1 (?l)/DNA Interactions.- 12. Summary.- References.- 3 PMR Studies of Secondary and Tertiary Structure of Transfer RNA in Solution.- 1. Introduction.- 1.1. PMR Observation of Base-Base Hydrogen Bonding Interactions.- 2. Analysis of Imino Proton Spectra.- 2.1. Integration of Low-Field Spectra: Number of Base Pairs.- 2.2. Identification of Resonances from Tertiary Interactions.- 2.3. Assignment of Common Resonances to Tertiary Interactions.- 2.4. Identification of and Assignment of Resonances from Secondary Structure Base Pairs.- 2.5. Ring Current Shifts on Tertiary Interactions.- 2.6. Summary of General PMR Methods and Results.- 3. Hydrogen Bonding of the 2? OH in tRNA.- 4. Metal Binding and Tertiary Structure.- 4.1. General Considerations.- 4.2. Location of Metal Binding Sites.- 4.3. Is Magnesium Special in Stabilizing the tRNA Tertiary Structure?.- 5. tRNA-Drug Interactions.- 6. Structure of Denatured tRNA.- 7. Interaction of tRNA with Enzymes.- 7.1. Effect of Aminoacylation on tRNA Structure.- 7.2. Interaction of tRNA with Aminoacyl Synthetases.- 7.3. Interaction of tRNA with the Elongation Factor Tu.- 8. Concluding Remarks.- References.- 4 Fluorine Magnetic Resonance in Biochemistry.- 1. Introduction.- 2. Characteristics of Fluorine Probes.- 2.1. Natural Occurrence of Carbon-Fluorine Bonds.- 2.2. Properties of Carbon-Fluorine Bonds.- 2.3. Biological Effects of Organofluorine Compounds.- 3. Fluorine Magnetic Resonance Experiments.- 3.1. Types of Experiments.- 4. Peptides and Proteins.- 4.1. Trifluoroacetylated Peptides and Amino Acids.- 4.2. Fluoroproline.- 4.3. Oxytocin.- 4.4. Angiotensin II.- 4.5. Thymidylate Synthetase Peptide.- 4.6. Insulin.- 4.7. Gene-5 Protein.- 4.8. Cytochrome c.- 4.9. Ribonuclease.- 4.10. Lysozyme:.- 4.11. Dihydrofolate Reductase.- 4.12. Histidine-Binding Protein J.- 4.13. Elastase.- 4.14. ?-Chymotrypsin.- 4.15. Papain.- 4.16. Acetylcholine Esterase.- 4.17. Concanavalin A.- 4.18. ?-Lactoglobulin A.- 4.19. Hemoglobin.- 4.20. Bovine Serum Albumin.- 4.21. Human Serum Albumin.- 4.22. Alkaline Phosphatase (E. coli).- 4.23. Human Carbonic Anhydrase C.- 4.24. Aspartate Transaminase.- 4.25. Glyceraldehyde-3?-phosphatase.- 4.26. Lactose Repressor.- 4.27. Pyruvate Kinase.- 4.28. Fluoride Ion.- 4.29. Histones H3 and H4.- 5. Nucleic Acids.- 6. Micelles, Membranes, and Membrane Models.- 7. Fluorocarbohydrates.- 8. Some Experimental Considerations.- 8.1. Preparation of Fluorinated Materials.- 8.2. Biosynthetic Incorporation.- 8.3. Instrumentation.- 9. Interpretation of Results.- 9.1. Chemical Shifts.- 9.2. Relaxation Parameters.- 9.3. Nuclear Overhauser Effects.- 10. Conclusions.- References.- 5 ESR of Free Radicals in Enzymatic Systems.- 1. Introduction.- 2. Methods used to Study Free Radical Intermediates.- 2.1. Rapid Freezing Technique.- 2.2. Flow Kinetic Techniques.- 3. Enzyme Free-Radical Intermediates: The Flavoenzymes.- 3.1. ESR Studies of Model Flavin Systems.- 3.2. ENDOR Studies of Model Flavin Systems.- 3.3. ESR Studies of Simple Flavoenzymes.- 3.4. ESR Studies of Complex Flavoenzymes.- 4. Substrate Free-Radical Intermediates in Enzymic Catalysis.- 4.1. ESR Studies on the Mechanism of Action of Peroxidases.- 4.2. ESR Studies on the Catalytic Mechanism of Vitamin-B12-Dependent Enzymes.- 4.3. ESR Studies on the Formation of the Superoxide Anion Radical.- 5. Summary.- References.- 6 Paramagnetic Intermediates in Photosynthetic Systems.- 1. Introduction.- 1.1. Preface.- 1.2. Photosynthetic Electron Transport.- 1.3. Electron Spin Resonance.- 2. Techniques and Methodologies.- 2.1. Photolysis Techniques.- 2.2. Cryogenic Spectroscopy.- 2.3. Redox Potentiometry.- 3. Paramagnetic Intermediates of the Reaction Center.- 3.1. Primary Donors.- 3.2. Primary Acceptors.- 3.3. Other Transient Components Associated with the Reaction Center.- 4. Secondary Electron Donors and Acceptors.- 4.1. Bacterial Systems.- 4.2. Green Plant and Algal Systems.- 5. Summary.- References.- 7 ESR of Copper in Biological Systems.- 1. Introduction.- 1.1. Copper Metabolism.- 1.2. ESR of Copper Proteins.- 2. Theory of the ESR due to Mononuclear Copper II.- 2.1. Introduction to Copper II ESR.- 2.2. The ESR of Copper II in Tetragonal and Orthorhombic Symmetry.- 2.3. Theory of the ESR of Blue Copper II Proteins.- 3. ESR Spectra due to Coupled Copper II Pairs.- 3.1. Introduction.- 3.2. Interactions between Copper II Pairs.- 3.3. Outline of the Theory of the ESR of Coupled Copper II Ion Pairs.- 4. ESR of Copper II in Plant and Animal Physiology.- 4.1. Copper Proteins in Bloodstreams.- 4.2. Cytochrome C Oxidase.- 4.3. L-Tryptophan-2,3-dioxygenase.- 4.4. Amine Oxidases.- 4.5. Dopamine-?-hydroxylase.- 4.6. Tyrosinase.- 4.7. Quercetinase.- 4.8. Laccases.- 4.9. Ascorbate Oxidase.- 4.10. Galactose Oxidase.- 4.11. Plastocyanins.- 4.12. Ribulose-1,5-diphosphate Carboxylase.- 4.13. Azurins.- 4.14. Stellacyanin and Umecyanin.- 4.15. Copper II Substituted into Systems of Biochemical Interest.- 4.16. ESR of Copper II in Tissue Material.- 4.17. Copper Proteins for which ESR Data Are Not Available.- 5. Conclusions.- References.

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