High-Resolution NMR Techniques in Organic Chemistry

High-Resolution NMR Techniques in Organic Chemistry, Third Edition describes the most important NMR spectroscopy techniques for the structure elucidation of organic molecules and the investigation of their behaviour in solution. Appropriate for advanced undergraduate and graduate students, research chemists and NMR facility managers, this thorough revision covers practical aspects of NMR techniques and instrumentation, data collection, and spectrum interpretation. It describes all major classes of one- and two-dimensional NMR experiments including homonuclear and heteronuclear correlations, the nuclear Overhauser effect, diffusion measurements, and techniques for studying protein–ligand interactions. A trusted authority on this critical expertise, High-Resolution NMR Techniques in Organic Chemistry, Third Edition is an essential resource for every chemist and NMR spectroscopist.

Organic Chemistry students and professionals who require NMR skills, NMR directors at academic and industry institutions

• Preface
• Chapter 1: Introduction
• 1.1 The development of high-resolution NMR
• 1.2 Modern high-resolution NMR and this book
• 1.3 Applying modern NMR techniques
• Chapter 2: Introducing High-Resolution NMR
  • 2.1 Nuclear spin and resonance
  • 2.2 The vector model of NMR
  • 2.3 Time and frequency domains
  • 2.4 Spin relaxation
  • 2.5 Mechanisms for relaxation
  • 2.6 Dynamic effects in NMR
• Chapter 3: Practical Aspects of High-Resolution NMR
  • 3.1 An overview of the NMR spectrometer
  • 3.2 Data acquisition and processing
  • 3.3 Preparing the sample
  • 3.4 Preparing the spectrometer
  • 3.5 Spectrometer calibrations
  • 3.6 Spectrometer performance tests
• Chapter 4: One-Dimensional Techniques
  • 4.1 Single-pulse experiment
  • 4.2 Spin-decoupling methods
  • 4.3 Spectrum editing with spin-echoes
  • 4.4 Sensitivity enhancement and spectrum editing
  • 4.5 Observing quadrupolar nuclei
• Chapter 5: Introducing Two-Dimensional and Pulsed Field Gradient NMR
• 5.1 Two-dimensional experiments
• 5.2 Practical aspects of 2D NMR
• 5.3 Coherence and coherence transfer
• 5.4 Gradient-selected spectroscopy
• Chapter 6: Correlations Through the Chemical Bond I: Homonuclear Shift Correlation
• 6.1 Correlation Spectroscopy: COSY
• 6.2 Total correlation spectroscopy: TOCSY
• 6.3 Correlating dilute spins: INADEQUATE
• 6.4 Correlating dilute spins via protons: ADEQUATE
• Chapter 7: Correlations Through the Chemical Bond II: Heteronuclear Shift Correlation
• 7.1 Introduction
• 7.2 Sensitivity
• 7.3 Heteronuclear single-bond correlations
• 7.4 Heteronuclear multiple-bond correlations
• 7.5 Heteronuclear X-detected correlations
• 7.6 Heteronuclear X–Y correlations
• 7.7 Parallel acquisition NMR with multiple receivers
• Chapter 8: Separating Shifts and Couplings: J-Resolved and Pure Shift Spectroscopy
  • 8.1 Introduction
  • 8.2 Heteronuclear J-resolved spectroscopy
  • 8.3 Homonuclear J-resolved spectroscopy
  • 8.4 ‘Indirect’ homonuclear J-resolved spectroscopy
  • 8.5 Pure shift broadband-decoupled 1H spectroscopy
• Chapter 9: Correlations Through Space: The Nuclear Overhauser Effect
• 9.1 Introduction
  Part I Theoretical Aspects
• 9.2 Defi nition of the NOE
• 9.3 Steady-State NOEs
• 9.4 Transient NOEs
• 9.5 Rotating Frame NOEs
  Part II Practical Aspects
• 9.6 Measuring Transient NOEs: NOESY
• 9.7 Measuring Rotating Frame NOEs: ROESY
• 9.8 Measuring Steady-State NOEs: NOE Difference
• 9.9 Measuring Heteronuclear NOEs: HOESY
• 9.10 Experimental Considerations for NOE Measurements
• 9.11 Measuring Chemical Exchange: EXSY
• 9.12 Residual Dipolar Couplings
• Chapter 10: Diffusion NMR Spectroscopy
  • 10.1 Introduction
  • 10.2 Measuring self-diffusion by NMR
  • 10.3 Practical aspects of diffusion NMR spectroscopy
  • 10.4 Applications of diffusion NMR spectroscopy
  • 10.5 Hybrid diffusion sequences
• Chapter 11: Protein–Ligand Screening by NMR
  • 11.1 Introduction
  • 11.2 Protein–ligand binding equilibria
  • 11.3 Resonance lineshapes and relaxation editing
  • 11.4 Saturation transfer difference
  • 11.5 Water-LOGSY
  • 11.6 Exchange-transferred nuclear Overhauser effects
  • 11.7 Competition ligand screening
  • 11.8 Protein observe methods
• Chapter 12: Experimental Methods
• 12.1 Composite pulses
• 12.2 Adiabatic and broadband pulses
• 12.3 Broadband decoupling and spin locking
• 12.4 Selective excitation and soft pulses
• 12.5 Solvent suppression
• 12.6 Suppression of zero-quantum coherences
• 12.7 Heterogeneous samples and magic angle spinning
• 12.8 Hyperpolarisation
• Chapter 13: Structure Elucidation and Spectrum Assignment
  • 13.1 1H NMR
  • 13.2 1H–13C edited HSQC
  • 13.3 1H–1H COSY and variants
  • 13.4 1H–1H TOCSY and variants
  • 13.5 13C NMR
  • 13.6 HMBC and variants
  • 13.7 Nuclear Overhauser effects
  • 13.8 Rationalization of 1H–1H coupling constants
  • 13.9 Summary
• Appendix
• Subject Index