NMR for Chemists and Biologists

<p>1. The basis of Nuclear Magnetic Resonance Spectroscopy<br>1.1. Introduction<br>1.2. Physical principles of NMR spectroscopy<br>1.2.1. The basis of NMR spectroscopy: a vector approach<br>1.2.2. The basis of NMR spectroscopy: a naïve quantum approach<br>1.2.3. The nuclei in NMR<br>1.3. Spin relaxation<br>1.3.1. Spin-lattice relaxation time<br>1.3.2. Spin-spin relaxation time<br>1.3.3. Sources of variation in local fields<br>1.4. Pulse techniques<br>1.4.1. How a pulse works: the time and frequency domains<br>1.4.2. Multipulse experiments: measurement of the T₁- and T₂-relaxation times as examples<br>1.5. Practical aspects of NMR<br>1.5.1. The magnet<br>1.5.2. The probe<br>1.5.3. The lock-system<br>1.5.4. The transmitter/receiver system: quadrature detection<br>1.5.5. The shim system<br>1.5.6. Pulse field gradients<br>1.5.7. Sample preparation<br>1.6. References </p><p>2. Spectroscopic parameters in Nuclear Magnetic Resonance<br>2.1. The chemical shift and the spectral intensity<br>2.1.1. The shielding screening constant<br>2.1.2. The chemical shift<br>2.1.3. Signal intensity<br>2.2. The scalar coupling constant<br>2.2.1. Spin-spin coupling2.2.2. How does spin-spin coupling occur?<br>2.2.3. Variations in the value of J<br>2.2.4. Spin-spin decoupling<br>2.3. The nuclear Overhauser effect<br>2.3.1. The basis of the NOE: a two spin system<br>2.3.2. NOEs in multi-spin systems<br>2.4. References  </p><p>3. Basic NMR experiments<br>3.1. Introduction<br>3.2. 1D NMR <br>3.2.1. Sensitivity and frequency<br>3.2.2. Acquisition and processing<br>3.2.3. 1D spectra of ¹H, ¹³C,³¹P and ¹⁹F<br>3.3. Multidimensional NMR<br>3.3.1. Generating dimensions in NMR<br>3.3.2. 2D data acquisition and processing <br>3.4. Homonuclear shift correlation: correlations through the chemical bond<br>3.4.1. COSY. Experiment interpretation and practical aspects<br>3.4.2. TOCSY. Practical aspects <br>3.4.3. Correlation for diluted spins: the INADEQUATE experiment. Double-quantum selection<br>3.5. Heteronuclear shift correlation: correlations through the chemical bond<br>3.5.1. Polarization transfer experiments: SPT and INEPT sequences; indirect spectroscopy<br>3.5.2. Heteronuclear single bond correlations: HSQC and HMQC<br>3.5.3. Double resonance experiments: homonuclear spin decoupling; heteronuclear double resonance and broadband decoupling<br>3.6. Correlations through space<br>3.6.1. Steady-state NOE<br>3.6.2. Kinetic or transient NOE<br>3.6.3. The 2D-NOESY sequence and practical aspects of the experiment<br>3.7. References </p><p>4. Biomolecular NMR<br>4.1. Introduction<br>4.2. Why biomolecules? Main applications<br>4.3. Structure of biomolecules<br>4.3.1. Homonuclear and heteronuclear (triple resonance) assignment in proteins<br>4.3.2. Nucleic acids<br>4.4. Biomolecular dynamics<br>4.4.1. Comparison with other spectroscopies and other structural biophysical techniques<br>4.4.2. Movements in the ps-s range <br>4.5. Biomolecular interactions (NMR in drug discovery)<br>4.5.1. Order of the affinities measured<br>4.5.2. Experiments in NMR screening <br>4.6. Other applications<br>4.6.1. Metabolomics<br>4.6.2. Solid state NMR and HR-MAS<br>4.7. References</p>