High-Resolution NMR Techniques in Organic Chemistry - Edition 3 - By Timothy D.W. Claridge Elsevier Inspection Copies

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High-Resolution NMR Techniques in Organic Chemistry,

Edition 3

By Timothy D.W. Claridge

Publication Date: 11 May 2016

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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.

About the author

By Timothy D.W. Claridge, University of Oxford, Oxford, UK

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

ISBN: 9780080999869

Page Count: 552

Retail Price : £66.99

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Wawer/Diehl, NMR Spectroscopy in Pharmaceutical Analysis, 9780444531735, Oct 2008, $131.00
Contreras, High Resolution NMR Spectroscopy: Understanding Molecules and Their Electronic Structures, 9780444594143, Aug 2013, $199.95
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Organic Chemistry students and professionals who require NMR skills, NMR directors at academic and industry institutions

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