High-Resolution NMR Techniques in Organic Chemistry
3rd Edition
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Description
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.
Readership
Organic Chemistry students and professionals who require NMR skills, NMR directors at academic and industry institutions
Table of Contents
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
Details
- No. of pages:
- 552
- Language:
- English
- Copyright:
- © Elsevier Science 2016
- Published:
- 11th May 2016
- Imprint:
- Elsevier Science
- Paperback ISBN:
- 9780080999869
- eBook ISBN:
- 9780080999937
About the Author
Timothy D.W. Claridge
Tim Claridge has over 25 years of practical experience in NMR Spectroscopy and is presently Professor of Magnetic Resonance and Director of NMR Spectroscopy for Organic Chemistry and Chemical Biology in the Department of Chemistry at the University of Oxford. His interest in NMR was ignited as an undergraduate student of Chemistry and Analytical Science whilst undertaking a year-long industrial placement in the spectroscopy laboratory of a leading pharmaceutical company. He subsequently completed a DPhil in protein NMR spectroscopy under the supervision of the late Andy Derome in the Dyson Perrins Laboratory at the University of Oxford. He then remained in Oxford and was appointed manager of the organic chemistry NMR facilities and in this capacity co-authored the undergraduate text "Introduction to Organic Spectroscopy (OUP)" with Prof Laurence Harwood and produced the first edition of "High-Resolution NMR Techniques in Organic Chemistry" (Pergamon Press). He became University Research Lecturer (Reader) in 2006, and was made a full Professor and a Fellow of the Royal Society of Chemistry (RSC) in 2014. He served for many years on the RSC NMR Discussion Group committee including as its Chairman for three years. He has co-authored over 170 research papers and his research interests focus broadly on the application of solution-state NMR methods for characterizing small molecules, and for studying their behavior and their interactions, especially as ligands for biological macromolecules.
Affiliations and Expertise
University of Oxford, Oxford, UK
