Fundamentals of Protein NMR Spectroscopy

Professor of Biological Sciences at Carnegie Mellon University. Professor Rule's research is directed at understanding inter-molecular interactions in biological systems. An understanding of these interactions is required if biological systems are to be comprehended at the molecular level. The combined tools of molecular biology, NMR spectroscopy and x-ray crystallography are used to provide important information to aid in our understanding of these interactions. Our research efforts have been directed at enzyme-substrate interactions, protein-lipid interactions, antibody-antigen interactions, and protein-nucleic acid interactions

NMR Spectroscopy.- Practical Aspects of Acquiring NMR Spectra.- to Signal Processing.- Quantum Mechanical Description of NMR.- Quantum Mechanical Description of a One Pulse Experiment.- The Density Matrix & Product Operators.- Scalar Coupling.- Coupled Spins: Density Matrix and Product Operator Formalism.- Two Dimensional Homonuclear J-Correlated Spectroscopy.- Two Dimensional Heteronuclear J-Correlated Spectroscopy.- Coherence Editing: Pulsed-Field Gradients and Phase Cycling.- Quadrature Detection in Multi-Dimensional NMR Spectroscopy.- Resonance Assignments: Homonuclear Methods.- Resonance Assignments: Heteronuclear Methods.- Practical Aspects of N-Dimensional Data Acquisition and Processing.- Dipolar Coupling.- Protein Structure Determination.- Exchange Processes.- Nuclear Spin Relaxation and Molecular Dynamics.