Numerous investigations over the years have illustrated the importance of physical methods, especially magnetic resonance, in the elucidation of the electronic ground states of 3d transition metal ion complexes. The results of these studies coupled with investigations on model compounds are being extended in very meaningful ways to provide electronic structural information in biological systems. In systems not readily amenable to investiga tion by single crystal X-ray diffraction these methods provide structural information as well. It was felt that a NATO Advanced Study Institute that…mehr
Numerous investigations over the years have illustrated the importance of physical methods, especially magnetic resonance, in the elucidation of the electronic ground states of 3d transition metal ion complexes. The results of these studies coupled with investigations on model compounds are being extended in very meaningful ways to provide electronic structural information in biological systems. In systems not readily amenable to investiga tion by single crystal X-ray diffraction these methods provide structural information as well. It was felt that a NATO Advanced Study Institute that brought together experts in theoretical aspects of magnetic resonance, experts in biology and experts in both areas would be extremely profitable for all parties attending the school. The enthusiastic response of the participants indicated that our objectives were accomplished to a high degree. We hope this pUblication of the proceedings will transmit, to some degree, the stimulating discussion of the Conference. The enormity of the area selected for this Conference can be appreciated by all. We the editors take full responsibility for the many omissions resulting from the imposed limitations of time and resources. Florence, July 1979 I. Bertini R. S. Drago PARTICIPANTS Andersen, J. P. Institute of Medical Biochemistry - University of Aarhus DK-8000 Aarhus C Denmark Andersson, I. Fachbereich 15. 2, Analytische und Biologische Chemie, Universitat des Saarlandes - D-6600 Saarbrucken 11 F. R. G. Basosi, R.
I: Pulse Techniques and Nuclear Spin Relaxation.- 1. Spin-Lattice and Spin-Spin Relaxation Mechanisms.- 2. Experimental Techniques for the Measurement of T1, T2, Tp, and the NOE.- 3. Two-Dimensional (2D) NMR Spectroscopy.- II: Architecture and Dynamics of Isotopically Labelled Macromolecules by Nuclear Magnetic Resonance Spectroscopy.- 1. Introduction.- 2. Red Blood Cell Suspensions.- 3. Structural Constituents of Cells.- 4. 13c Labelled Enzymes: Dihydrofolate Reductase.- 5. Concluding Remarks.- III: Contact and Dipolar NMR Shifts: Theory and Applications.- 1. Introduction.- 2. Contact Shifts.- 3. Dipolar Shifts.- IV: Solvent Nuclear Magnetic Relaxation Dispersion (NMRD) in Solutions of Paramagnetic Proteins. A Critical Analysis, by Example.- 1. Introduction.- 2. Concanavalin A Data.- 3. Traditional SBM Theory.- 4. Comparison of Data with Traditional SBM Theory.- 5. Another Approach to SBM.- 6. Implications of the New View.- 7. Critique of the Parameters.- 8. Discussion.- V: Multiple Pulse 1H NMR Experiments for Structural Studies of Hemoproteins.- 1. Introduction.- 2. Multiple Pulse Experiments.- 3. Recent Applications of Multiple Pulse Experiments for Structural Studies of Hemoproteins.- VI: Nuclear Magnetic Resonance Studies of Paramagnetic Proteins.- 1. Introduction.- 2. Paramagnetic Shifts.- 3. Hemes.- VII : Paramagnetic Ions as Relaxation Probes in Biological Systems.- 1. Introduction.- 2. Theory.- 3. Applications.- 4. Conclusions.- VIII: Theory of Electron Spin Resonance.- 1. S = 1/2 Systems.- 2. S = 3/2 and 5/2 Systems.- 3. Pseudo S = 1/2 Systems.- IX: The Electronic Ground State of 3d Metal Ions with Respect to the ESR and NMR Experiment.- 1. Survey of General Theory.- 2. The ESR Experiment.- 3. The NMR Experiment.- X: EPR of Iron in Biological Systems.- 1. Introduction.- 2. High-Spin Ferrous; S =2.- 3. Low-Spin Ferric; S = 1/2.- 4. High-Spin Ferric; S = 5/2.- 5. Spin Equilibria; S = 5/2, 1/2.- 6. Intermediate Spin; S = 3/2.- 7. Non-Haem Iron Sulphur Clusters.- XI: ESR and NMR Spectra of Exchange Coupled Metal Ions.- 1. The Nature of the Exchange Interaction.- 2. Effect of Exchange on the Magnetic Resonance Spectra.- XII: Iron Sulfur Proteins: Combined Mössbauer and EPR Studies.- 1. Introduction.- 2. Some Basic Features of 57Fe Mössbauer Spectroscopy.- 3. Paramagnetic Hyperfine Structure and Connection with EPR Data.- 4. Mossbauer and EPR Studies of Nitrogenase.- XIII: The Spin-Pairing Model for the Binding of Dioxygen to Transition Metal Complexes.- 1. Introduction.- 2. The Spin-Pairing Model.- 3. Electron Transfer Analysis.- 4. The Isotropic Cobalt Hyperfine Coupling Constant.- 5. Relevance of the Spin-Pairing Model to Hemoglobin Cooperativity.- XIV: EPR Studies of Copper Centers in Proteins.- 1. Introduction.- 2. Copper-Proteins Containing all the Copper in a Form that is not Detected by EPR in the Native States.- 3. Copper-Proteins where all the Copper Exists as an EPR-Detectable Form: the Mononuclear Cu( II) -Proteins.- 4. Copper-Proteins with Partially EPR-Detectable Copper: the Proteins with Multiple Copper Centers that Reduce 02 to H20.- XV: The Binding of Divalent Ions to Transfer Nucleic Acids.- 1. Introduction.- 2. EPR Titration of Manganese Binding to tRNA.- 3. EPR of Bound Manganese.- 4. Phosphorus NMR and Relaxation of tRNA.- 5. A Polyelectrolyte Theory of Binding of Manganese to tRNA.- XVI: Physical Studies of Azurin and Some Metal Replaced Derivatives.- 1. Introduction.- 2. Spectral Studies of Azurin and its Metal Replaced Derivatives.- 3. Summary.- XVII: Physical Aspects of the Spin Labelling Technique.- 1.Nitroxide Radicals can give Information about Motion.- 2. Conventional EPR: 10-10
I: Pulse Techniques and Nuclear Spin Relaxation.- 1. Spin-Lattice and Spin-Spin Relaxation Mechanisms.- 2. Experimental Techniques for the Measurement of T1, T2, Tp, and the NOE.- 3. Two-Dimensional (2D) NMR Spectroscopy.- II: Architecture and Dynamics of Isotopically Labelled Macromolecules by Nuclear Magnetic Resonance Spectroscopy.- 1. Introduction.- 2. Red Blood Cell Suspensions.- 3. Structural Constituents of Cells.- 4. 13c Labelled Enzymes: Dihydrofolate Reductase.- 5. Concluding Remarks.- III: Contact and Dipolar NMR Shifts: Theory and Applications.- 1. Introduction.- 2. Contact Shifts.- 3. Dipolar Shifts.- IV: Solvent Nuclear Magnetic Relaxation Dispersion (NMRD) in Solutions of Paramagnetic Proteins. A Critical Analysis, by Example.- 1. Introduction.- 2. Concanavalin A Data.- 3. Traditional SBM Theory.- 4. Comparison of Data with Traditional SBM Theory.- 5. Another Approach to SBM.- 6. Implications of the New View.- 7. Critique of the Parameters.- 8. Discussion.- V: Multiple Pulse 1H NMR Experiments for Structural Studies of Hemoproteins.- 1. Introduction.- 2. Multiple Pulse Experiments.- 3. Recent Applications of Multiple Pulse Experiments for Structural Studies of Hemoproteins.- VI: Nuclear Magnetic Resonance Studies of Paramagnetic Proteins.- 1. Introduction.- 2. Paramagnetic Shifts.- 3. Hemes.- VII : Paramagnetic Ions as Relaxation Probes in Biological Systems.- 1. Introduction.- 2. Theory.- 3. Applications.- 4. Conclusions.- VIII: Theory of Electron Spin Resonance.- 1. S = 1/2 Systems.- 2. S = 3/2 and 5/2 Systems.- 3. Pseudo S = 1/2 Systems.- IX: The Electronic Ground State of 3d Metal Ions with Respect to the ESR and NMR Experiment.- 1. Survey of General Theory.- 2. The ESR Experiment.- 3. The NMR Experiment.- X: EPR of Iron in Biological Systems.- 1. Introduction.- 2. High-Spin Ferrous; S =2.- 3. Low-Spin Ferric; S = 1/2.- 4. High-Spin Ferric; S = 5/2.- 5. Spin Equilibria; S = 5/2, 1/2.- 6. Intermediate Spin; S = 3/2.- 7. Non-Haem Iron Sulphur Clusters.- XI: ESR and NMR Spectra of Exchange Coupled Metal Ions.- 1. The Nature of the Exchange Interaction.- 2. Effect of Exchange on the Magnetic Resonance Spectra.- XII: Iron Sulfur Proteins: Combined Mössbauer and EPR Studies.- 1. Introduction.- 2. Some Basic Features of 57Fe Mössbauer Spectroscopy.- 3. Paramagnetic Hyperfine Structure and Connection with EPR Data.- 4. Mossbauer and EPR Studies of Nitrogenase.- XIII: The Spin-Pairing Model for the Binding of Dioxygen to Transition Metal Complexes.- 1. Introduction.- 2. The Spin-Pairing Model.- 3. Electron Transfer Analysis.- 4. The Isotropic Cobalt Hyperfine Coupling Constant.- 5. Relevance of the Spin-Pairing Model to Hemoglobin Cooperativity.- XIV: EPR Studies of Copper Centers in Proteins.- 1. Introduction.- 2. Copper-Proteins Containing all the Copper in a Form that is not Detected by EPR in the Native States.- 3. Copper-Proteins where all the Copper Exists as an EPR-Detectable Form: the Mononuclear Cu( II) -Proteins.- 4. Copper-Proteins with Partially EPR-Detectable Copper: the Proteins with Multiple Copper Centers that Reduce 02 to H20.- XV: The Binding of Divalent Ions to Transfer Nucleic Acids.- 1. Introduction.- 2. EPR Titration of Manganese Binding to tRNA.- 3. EPR of Bound Manganese.- 4. Phosphorus NMR and Relaxation of tRNA.- 5. A Polyelectrolyte Theory of Binding of Manganese to tRNA.- XVI: Physical Studies of Azurin and Some Metal Replaced Derivatives.- 1. Introduction.- 2. Spectral Studies of Azurin and its Metal Replaced Derivatives.- 3. Summary.- XVII: Physical Aspects of the Spin Labelling Technique.- 1.Nitroxide Radicals can give Information about Motion.- 2. Conventional EPR: 10-10
Es gelten unsere Allgemeinen Geschäftsbedingungen: www.buecher.de/agb
Impressum
www.buecher.de ist ein Shop der buecher.de GmbH & Co. KG Bürgermeister-Wegele-Str. 12, 86167 Augsburg Amtsgericht Augsburg HRA 13309
