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
