NMR for Chemists and Biologists

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