The critically acclaimed laboratory standard for forty years, <b>Methods in Enzymology</b> is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerlyawaited, frequently consulted, and praised by researchers and reviewers alike. More than 2
Nuclear Magnetic Resonance
✍ Scribed by Peter John Hore
- Publisher
- Oxford University Press
- Year
- 1995
- Tongue
- English
- Leaves
- 100
- Series
- Oxford Chemistry Primers 32
- Category
- Library
No coin nor oath required. For personal study only.
✦ Table of Contents
NUCLEAR MAGNETIC RESONANCE......Page 1
Oxford Chemistry Primers 32......Page 2
Title......Page 3
Copyright......Page 4
Preface......Page 5
Contents......Page 6
Chapter 1. Introduction......Page 9
Space quantization......Page 10
Nuclear magnetization......Page 11
Resonance frequencies......Page 12
Populations of energy levels......Page 13
Widths of NMR lines......Page 14
Experimental methods......Page 15
2.1 Nuclear shielding......Page 16
Measuring chemical shifts......Page 17
Examples......Page 18
2.2 Origin of chemical shifts......Page 21
2.3 Contributions to nuclear shielding......Page 22
Local diamagnetic shifts......Page 23
Local paramagnetic shifts......Page 24
Neighbouring groups......Page 25
Other sources of chemical shifts......Page 28
3.1 Effect on NMR spectra......Page 30
3.2 Multiplet patterns......Page 32
Coupling to two inequivalent spin-1/2 nuclei (AMX)......Page 33
Coupling to three equivalent spin-1/2 nuclei (AX3)......Page 34
Coupling involving I > 1/2 nuclei......Page 35
Equivalent nuclei......Page 36
3.3 Examples......Page 37
3.4 Equivalent nuclei......Page 39
3.5 Strong coupling......Page 40
Contact interaction......Page 42
Indirect coupling between nuclei......Page 43
One-bond and two-bond couplings......Page 45
Three-bond couplings......Page 46
Long-range couplings......Page 47
Magnetic field of a point dipole......Page 48
Dipolar interaction between nuclei in solids......Page 49
Dipolar interaction between nuclei in liquids......Page 50
Chapter 4. Chemical exchange......Page 52
Slow exchange......Page 53
Fast exchange......Page 54
NMR time-scale......Page 55
4.2 Unsymmetrical two-site exchange......Page 56
Cis-decals—ring inversion......Page 57
Bullvalene—degenerate rearrangement......Page 58
(η^4 —C8H8)Ru(CO)3—mechanism of rearrangement......Page 60
Ethanol—proton exchange......Page 61
Motion of tyrosine side-chains in proteins......Page 62
The origin of spin–lattice relaxation......Page 64
5.2 Rotational motion in liquids......Page 65
5.3 Spin–lattice relaxation again......Page 67
5.4 The nuclear Overhauser effect......Page 69
5.5 Spin–spin relaxation......Page 72
5.6 Quadrupolar relaxation......Page 73
CH and CH2 carbons......Page 75
Protein structure determination......Page 76
Methyl group internal rotation......Page 77
Alkyl chains......Page 78
Solid benzene......Page 79
6.1 Instrumental requirements......Page 80
The rotating frame......Page 82
Radiofrequency pulses......Page 83
Free precession and relaxation......Page 84
The NMR spectrum......Page 85
Why bother?......Page 86
Inversion recovery—measurement of T_1......Page 87
Spin echoes—measurement of T_2......Page 88
6.4 Two-dimensional NMR......Page 89
Nuclear Overhauser effect spectroscopy (NOESY)......Page 90
Correlated spectroscopy (COSY)......Page 92
Bibliography......Page 96
Index......Page 97
Back Cover......Page 100
📜 SIMILAR VOLUMES
Nuclear magnetic resonance spectroscopy is an enormously powerful and versatile physical method for investigating the structure and dynamics of molecules. This text provides a clear, concise introduction to the physical principles of NMR, and the interactions that determine the appearance of NMR spe
Nuclear magnetic resonance spectroscopy is an enormously powerful and versatile physical method for investigating the structure and dynamics of molecules. This text provides a clear, concise introduction to the physical principles of NMR, and the interactions that determine the appearance of NMR spe