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  • Produktbild: Biological Magnetic Resonance
  • Produktbild: Biological Magnetic Resonance
Band 1

Biological Magnetic Resonance

Aus der Reihe Biological Magnetic Resonance

51,99 €

inkl. gesetzl. MwSt., Versandkostenfrei

Beschreibung

Produktdetails

Einband

Taschenbuch

Erscheinungsdatum

06.02.2013

Herausgeber

Lawrence Berliner

Verlag

Springer Us

Seitenzahl

345

Maße (L/B/H)

22,9/15,2/2 cm

Gewicht

527 g

Auflage

Softcover reprint of the original 1st ed. 1978

Sprache

Englisch

ISBN

978-1-4615-6536-9

Beschreibung

Produktdetails

Einband

Taschenbuch

Erscheinungsdatum

06.02.2013

Herausgeber

Lawrence Berliner

Verlag

Springer Us

Seitenzahl

345

Maße (L/B/H)

22,9/15,2/2 cm

Gewicht

527 g

Auflage

Softcover reprint of the original 1st ed. 1978

Sprache

Englisch

ISBN

978-1-4615-6536-9

Herstelleradresse

Springer-Verlag KG
Sachsenplatz 4-6
1201 Wien
AT

Email: GPSR Kontakt

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  • Produktbild: Biological Magnetic Resonance
  • Produktbild: Biological Magnetic Resonance
  • 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.