Nuclear magnetic Resonance in biochemistry

Nuclear Magnetic Resonance in Biochemistry: Principles and Applications focuses on the principles and applications of nuclear magnetic resonance (NMR) in biochemistry. Topics covered include experimental methods in NMR; the mechanisms of NMR relaxation; chemical and paramagnetic shifts; spin-spin splitting; the use of NMR in investigations of biopolymers and biomolecular interactions; and molecular dynamics in biological and biochemical systems. This text is comprised of eight chapters; the first of which gives an overview of NMR spectroscopy and its use in studies of biological systems. The next two chapters discuss the theoretical basis for NMR applications in biochemistry, with emphasis on Bloch equations, quantum mechanics, correlation function and correlation time, double resonance, and chemical exchange. The reader is then introduced to the basis for chemical shifts and spin-spin splitting, along with several examples of the use of these NMR parameters in studies of small molecule interactions and structure. The experimental apparatus and procedures employed in NMR studies, Fourier transform NMR, and NMR spectral parameters of small molecules interacting with macromolecules are also considered. The book highlights the information obtainable from the spectra of biopolymers, and then concludes with a chapter on NMR investigations of the state of motion of lipids in membranes and model membranes; water in macromolecular and cellular systems; and sodium ion in biological tissue. This book is intended primarily for chemists, biochemists, biophysicists, and molecular biologists, as well as graduate students.

Table of Contents:
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