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[资源] NMR Spectroscopy Explained: Simplified Theory, Applications and

NMR Spectroscopy Explained: Simplified Theory, Applications and Examples for Organic Chemistry and Structural Biology
By Neil E. Jacobsen

Publisher:  Wiley-Interscience
Number Of Pages:  688
Publication Date:  2007-08-24
ISBN / ASIN:  0471730963

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Book Description:

NMR Spectroscopy Explained : Simplified Theory, Applications and Examples for Organic Chemistry and Structural Biology provides a fresh, practical guide to NMR for both students and practitioners, in a clearly written and non-mathematical format. It gives the reader an intermediate level theoretical basis for understanding laboratory applications, developing concepts gradually within the context of examples and useful experiments.

Introduces students to modern NMR as applied to analysis of organic compounds.
Presents material in a clear, conversational style that is appealing to students.
Contains comprehensive coverage of how NMR experiments actually work.
Combines basic ideas with practical implementation of the spectrometer.
Provides an intermediate level theoretical basis for understanding laboratory experiments.
Develops concepts gradually within the context of examples and useful experiments.
Introduces the product operator formalism after introducing the simpler (but limited) vector model.

Preface xi
Acknowledgments xv
1 Fundamentals of NMR Spectroscopy in Liquids 1
1.1 Introduction to NMR Spectroscopy, 1
1.2 Examples: NMR Spectroscopy of Oligosaccharides and Terpenoids, 12
1.3 Typical Values of Chemical Shifts and Coupling Constants, 27
1.4 Fundamental Concepts of NMR Spectroscopy, 30
2 Interpretation of Proton (1H) NMR Spectra 39
2.1 Assignment, 39
2.2 Effect of Bo Field Strength on the Spectrum, 40
2.3 First-Order Splitting Patterns, 45
2.4 The Use of 1H–1H Coupling Constants to Determine Stereochemistry
and Conformation, 52
2.5 Symmetry and Chirality in NMR, 54
2.6 The Origin of the Chemical Shift, 56
2.7 J Coupling to Other NMR-Active Nuclei, 61
2.8 Non-First-Order Splitting Patterns: Strong Coupling, 63
2.9 Magnetic Equivalence, 71
3 NMR Hardware and Software 74
3.1 Sample Preparation, 75
3.2 Sample Insertion, 77
3.3 The Deuterium Lock Feedback Loop, 78
vi CONTENTS
3.4 The Shim System, 81
3.5 Tuning and Matching the Probe, 88
3.6 NMR Data Acquisition and Acquisition Parameters, 90
3.7 Noise and Dynamic Range, 108
3.8 Special Topic: Oversampling and Digital Filtering, 110
3.9 NMR Data Processing—Overview, 118
3.10 The Fourier Transform, 119
3.11 Data Manipulation Before the Fourier Transform, 122
3.12 Data Manipulation After the Fourier Transform, 126
4 Carbon-13 (13C) NMR Spectroscopy 135
4.1 Sensitivity of 13C, 135
4.2 Splitting of 13C Signals, 135
4.3 Decoupling, 138
4.4 Heteronuclear Decoupling: 1H Decoupled 13C Spectra, 139
4.5 Decoupling Hardware, 145
4.6 Decoupling Software: Parameters, 149
4.7 The Nuclear Overhauser Effect (NOE), 150
4.8 Heteronuclear Decoupler Modes, 152
5 NMR Relaxation—Inversion-Recovery and the Nuclear
Overhauser Effect (NOE) 155
5.1 The Vector Model, 155
5.2 One Spin in a Magnetic Field, 155
5.3 A Large Population of Identical Spins: Net Magnetization, 157
5.4 Coherence: Net Magnetization in the x–y Plane, 161
5.5 Relaxation, 162
5.6 Summary of the Vector Model, 168
5.7 Molecular Tumbling and NMR Relaxation, 170
5.8 Inversion-Recovery: Measurement of T1 Values, 176
5.9 Continuous-Wave Low-Power Irradiation of One Resonance, 181
5.10 Homonuclear Decoupling, 182
5.11 Presaturation of Solvent Resonance, 185
5.12 The Homonuclear Nuclear Overhauser Effect (NOE), 187
5.13 Summary of the Nuclear Overhauser Effect, 198
6 The Spin Echo and the Attached Proton Test (APT) 200
6.1 The Rotating Frame of Reference, 201
6.2 The Radio Frequency (RF) Pulse, 203
6.3 The Effect of RF Pulses, 206
6.4 Quadrature Detection, Phase Cycling, and the Receiver Phase, 209
6.5 Chemical Shift Evolution, 212
6.6 Scalar (J) Coupling Evolution, 213
6.7 Examples of J-coupling and Chemical Shift Evolution, 216
6.8 The Attached Proton Test (APT), 220
6.9 The Spin Echo, 226
6.10 The Heteronuclear Spin Echo: Controlling J-Coupling Evolution
and Chemical Shift Evolution, 232
7 Coherence Transfer: INEPT and DEPT 238
7.1 Net Magnetization, 238
7.2 Magnetization Transfer, 241
7.3 The Product Operator Formalism: Introduction, 242
7.4 Single Spin Product Operators: Chemical Shift Evolution, 244
7.5 Two-Spin Operators: J-coupling Evolution and Antiphase Coherence, 247
7.6 The Effect of RF Pulses on Product Operators, 251
7.7 INEPT and the Transfer of Magnetization from 1H to 13C, 253
7.8 Selective Population Transfer (SPT) as a Way of Understanding
INEPT Coherence Transfer, 257
7.9 Phase Cycling in INEPT, 263
7.10 Intermediate States in Coherence Transfer, 265
7.11 Zero- and Double-Quantum Operators, 267
7.12 Summary of Two-Spin Operators, 269
7.13 Refocused INEPT: Adding Spectral Editing, 270
7.14 DEPT: Distortionless Enhancement by Polarization Transfer, 276
7.15 Product Operator Analysis of the DEPT Experiment, 283
8 Shaped Pulses, Pulsed Field Gradients, and Spin Locks:
Selective 1D NOE and 1D TOCSY 289
8.1 Introducing Three New Pulse Sequence Tools, 289
8.2 The Effect of Off-Resonance Pulses on Net Magnetization, 291
8.3 The Excitation Profile for Rectangular Pulses, 297
8.4 Selective Pulses and Shaped Pulses, 299
8.5 Pulsed Field Gradients, 301
8.6 Combining Shaped Pulses and Pulsed Field Gradients:
“Excitation Sculpting”, 308
8.7 Coherence Order: Using Gradients to Select a Coherence Pathway, 316
8.8 Practical Aspects of Pulsed Field Gradients and Shaped Pulses, 319
8.9 1D Transient NOE using DPFGSE, 321
8.10 The Spin Lock, 333
8.11 Selective 1D ROESY and 1D TOCSY, 338
8.12 Selective 1D TOCSY using DPFGSE, 343
8.13 RF Power Levels for Shaped Pulses and Spin Locks, 348
viii CONTENTS
9 Two-Dimensional NMR Spectroscopy:
HETCOR, COSY, and TOCSY 353
9.1 Introduction to Two-Dimensional NMR, 353
9.2 HETCOR: A 2D Experiment Created from the 1D INEPT Experiment, 354
9.3 A General Overview of 2D NMR Experiments, 364
9.4 2D Correlation Spectroscopy (COSY), 370
9.5 Understanding COSY with Product Operators, 386
9.6 2D TOCSY (Total Correlation Spectroscopy), 393
9.7 Data Sampling in t1 and the 2D Spectral Window, 398
10 Advanced NMR Theory: NOESY and DQF-COSY 408
10.1 Spin Kinetics: Derivation of the Rate Equation for Cross-Relaxation, 409
10.2 Dynamic Processes and Chemical Exchange in NMR, 414
10.3 2D NOESY and 2D ROESY, 425
10.4 Expanding Our View of Coherence: Quantum Mechanics
and Spherical Operators, 439
10.5 Double-Quantum Filtered COSY (DQF-COSY), 447
10.6 Coherence Pathway Selection in NMR Experiments, 450
10.7 The Density Matrix Representation of Spin States, 469
10.8 The Hamiltonian Matrix: Strong Coupling and Ideal Isotropic
(TOCSY) Mixing, 478
11 Inverse Heteronuclear 2D Experiments: HSQC, HMQC, and HMBC 489
11.1 Inverse Experiments: 1H Observe with 13C Decoupling, 490
11.2 General Appearance of Inverse 2D Spectra, 498
11.3 Examples of One-Bond Inverse Correlation (HMQC and HSQC)
Without 13C Decoupling, 501
11.4 Examples of Edited, 13C-Decoupled HSQC Spectra, 504
11.5 Examples of HMBC Spectra, 509
11.6 Structure Determination Using HSQC and HMBC, 517
11.7 Understanding the HSQC Pulse Sequence, 522
11.8 Understanding the HMQC Pulse Sequence, 533
11.9 Understanding the Heteronuclear Multiple-Bond Correlation
(HMBC) Pulse Sequence, 535
11.10 Structure Determination by NMR—An Example, 538
12 Biological NMR Spectroscopy 551
12.1 Applications of NMR in Biology, 551
12.2 Size Limitations in Solution-State NMR, 553
12.3 Hardware Requirements for Biological NMR, 558
12.4 Sample Preparation and Water Suppression, 564
12.5 1H Chemical Shifts of Peptides and Proteins, 570
12.6 NOE Interactions Between One Residue and the Next Residue in
the Sequence, 577
12.7 Sequence-Specific Assignment Using Homonuclear 2D Spectra, 580
12.8 Medium and Long-Range NOE Correlations, 586
12.9 Calculation of 3D Structure Using NMR Restraints, 590
12.10 15N-Labeling and 3D NMR, 596
12.11 Three-Dimensional NMR Pulse Sequences: 3D HSQC–TOCSY
and 3D TOCSY–HSQC, 601
12.12 Triple-Resonance NMR on Doubly-Labeled (15N, 13C) Proteins, 610
12.13 New Techniques for Protein NMR: Residual Dipolar Couplings
and Transverse Relaxation Optimized Spectroscopy (TROSY), 621
Appendix A: A Pictorial Key to NMR Spin States 627
Appendix B: A Survey of Two-Dimensional NMR Experiments 634
Index 643
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