Nuclear magnetic Resonance in biochemistry

Preface Chapter 1 Introduction 1.1. Magnetic Properties of Nuclei 1.2. Magnetic Resonance 1.3. NMR Relaxation 1.4. Chemical Shift and Shielding 1.5. Spin-Spin Splitting 1.6. General Features of the NMR Spectrum References Chapter 2 Principles of Nuclear Magnetic Resonance 2.1. Classical Description—Bloch Equations 2.2. Quantum Mechanical Description of NMR 2.3. Correlation Function and Correlation Time 2.4. Relaxation Mechanisms 2.5. Double Resonance 2.6. Chemical Exchange References Chapter 3 Chemical Shifts and Structure 3.1. Shielding 3.2. Chemical Shifts 3.3. Paramagnetic Shifts ReferencesChapter 4 Spin-Spin Splitting and Structure 4.1. Origin of Spin-Spin Splitting 4.2. Analysis of NMR Spectra 4.3. Molecular Structure References Chapter 5 Experimental Methods 5.1. Detection of Nuclear Magnetic Resonance 5.2. High-Resolution Continuous Wave Spectrometer 5.3. Pulsed NMR Spectrometer 5.4. Fourier Transform NMR Spectrometer 5.5. Multiple Irradiation 5.6. Correlation Spectroscopy 5.7. Relaxation Time Measurements 5.8. Self-Diffusion Coefficient Measurements 5.9. Multiple-Pulse NMR Experiments 5.10. Sample Considerations References Chapter 6 NMR Studies of Biomolecular Interactions 6.1. Chemical Exchange 6.2. Paramagnetic Probes 6.3. Quadrupolar Nuclei 6.4. Binding of Small Diamagnetic Molecules to Macromolecules 6.5. Application of the Intermolecular Nuclear Overhauser Effect 6.6. Application of Chemically Induced Dynamic Nuclear Polarization References Chapter 7 NMR Spectra of Biopolymers 7.1. Proteins and Polypeptides 7.2. Nucleic Acids and Polynucleotides 7.3. Polysaccharides ReferencesChapter 8 Molecular Dynamics in Biological and Biochemical Systems 8.1. Membranes and Membrane Models 8.2. Water in Biochemical and Biological Systems 8.3. State of Sodium and Potassium Ions in Biological Tissue References Appendix 1 List of Symbols Appendix 2 Table of Nuclear Properties Subject Index