High-Resolution NMR Techniques in Organic Chemistry - 3rd Edition - ISBN: 9780080999869, 9780080999937

High-Resolution NMR Techniques in Organic Chemistry

3rd Edition

Authors: Timothy D.W. Claridge
eBook ISBN: 9780080999937
Paperback ISBN: 9780080999869
Imprint: Elsevier Science
Published Date: 11th May 2016
Page Count: 552
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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

  • 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

Details

No. of pages:
552
Language:
English
Copyright:
© Elsevier Science 2016
Published:
Imprint:
Elsevier Science
eBook ISBN:
9780080999937
Paperback ISBN:
9780080999869

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