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? Which experiment can best yield the desired information?
? How must the chosen experiment be performed?
? How does one read the required information from the spectrum?
? How does this particular pulse sequence work?
? Which other experiments give similar information?
This third edition of the book, following its two highly successful predecessors, has been revised and expanded to 206 experiments. They are organized in 15 chapters, covering test procedures and routine spectra, variable temperature measurements, the use of auxiliary reagents, 1D multipulse experiments, spectra of heteronuclides, and the application of selective pulses. The second and third dimensions are introduced using pulsed field gradients, and experiments on solid state materials are described. A key part describes 3D experiments on the protein ubiquitin with 76 amino acids.
What is new in this third edition?
1. 24 new experiments have been inserted into the 14 chapters that were in the 2nd edition, e.g., alpha/beta-SELINCOR-TOCSY, WET, DOSY, ct-COSY, HMSC, HSQC with adiabatic pulses, HETLOC. J-resolved HMBC, (1,1)- and (1,n)-ADEQUATE, STD, REDOR, and HR-MAS.
2. 20 new protein NMR experiments have been specially devised and are collected in the newly added Chapter 15, ProteinNMR, for which one needs a special model sample: fully 13C- and 15N-labeled human ubiquitin. Techniques used include the constant time principle, the PEP method, filters, gradient selection, and the echo/anti-echo procedure.
The guide has been written by experts in this field, following the principle of learning by doing: all the experiments have been specially performed for this book, exactly as described and shown in the spectra that are reproduced. Being a reference source and work-book for the NMR laboratory as well as a textbook, it is a must for every scientist working with NMR, as well as for students preparing for their laboratory courses
? Which experiment can best yield the desired information?
? How must the chosen experiment be performed?
? How does one read the required information from the spectrum?
? How does this particular pulse sequence work?
? Which other experiments give similar information?
This third edition of the book, following its two highly successful predecessors, has been revised and expanded to 206 experiments. They are organized in 15 chapters, covering test procedures and routine spectra, variable temperature measurements, the use of auxiliary reagents, 1D multipulse experiments, spectra of heteronuclides, and the application of selective pulses. The second and third dimensions are introduced using pulsed field gradients, and experiments on solid state materials are described. A key part describes 3D experiments on the protein ubiquitin with 76 amino acids.
What is new in this third edition?
1. 24 new experiments have been inserted into the 14 chapters that were in the 2nd edition, e.g., alpha/beta-SELINCOR-TOCSY, WET, DOSY, ct-COSY, HMSC, HSQC with adiabatic pulses, HETLOC. J-resolved HMBC, (1,1)- and (1,n)-ADEQUATE, STD, REDOR, and HR-MAS.
2. 20 new protein NMR experiments have been specially devised and are collected in the newly added Chapter 15, ProteinNMR, for which one needs a special model sample: fully 13C- and 15N-labeled human ubiquitin. Techniques used include the constant time principle, the PEP method, filters, gradient selection, and the echo/anti-echo procedure.
The guide has been written by experts in this field, following the principle of learning by doing: all the experiments have been specially performed for this book, exactly as described and shown in the spectra that are reproduced. Being a reference source and work-book for the NMR laboratory as well as a textbook, it is a must for every scientist working with NMR, as well as for students preparing for their laboratory courses
Stefan Berger was intrigued by NMR after having won a bottle of beer during an introductory course in organic NMR led by Professor H. Suhr at the University of Tübingen in 1968. After completing a PhD thesis with Professor Anton Rieker, in 1973 he joined Professor J. D. Roberts at Caltech for postdoctoral work, where he also met Professor D.M. Grant and Professor D. Seebach, who were then guest professors in Pasadena. This period was decisive to try a Habilitation in NMR spectroscopy, which was achieved at the University Marburg. At the University Leipzig his aim is to combine methodological development of NMR and its application to bioorganic problems.
Preface v
Chapter 1 The NMR Spectrometer 1
1.1 Components of an NMR Spectrometer 1
1.1.1 The Magnet 1
1.1.2 The Spectrometer Cabinet 2
1.1.3 The Computer 3
1.1.4 Maintenance 3
1.2 Tuning a Probe-Head 3
1.3 The Lock Channel 4
1.4 The Art of Shimming 6
1.4.1 The Shim Gradients 6
1.4.2 The Shimming Procedure 8
1.4.3 Gradient Shimming 11
Chapter 2 Determination of Pulse-Duration 14
Exp. 2.1: Determination of the 90° 1H Transmitter Pulse-Duration 15
Exp. 2.2: Determination of the 90° 13C Transmitter Pulse-Duration 18
Exp. 2.3: Determination of the 90° 1H Decoupler Pulse-Duration 21
Exp. 2.4: The 90° 1H Pulse with Inverse Spectrometer Configuration 24
Exp. 2.5: The 90° 13C Decoupler Pulse with Inverse Configuration 27
Exp. 2.6: Composite Pulses 30
Exp. 2.7: Radiation Damping 33
Exp. 2.8: Pulse and Receiver Phases 36
Exp. 2.9: Determination of Radiofrequency Power 39
Chapter 3 Routine NMR Spectroscopy and Standard Tests 43
Exp. 3.1: The Standard 1H NMR Experiment 44
Exp. 3.2: The Standard 13C NMR Experiment 49
Exp. 3.3: The Application of Window Functions 54
Exp. 3.4: Computer-Aided Spectral Analysis 58
Exp. 3.5: Line Shape Test for 1H NMR Spectroscopy 61
Exp. 3.6: Resolution Test for 1H NMR Spectroscopy 64
Exp. 3.7: Sensitivity Test for 1H NMR Spectroscopy 67
Exp. 3.8: Line Shape Test for 13C NMR Spectroscopy 70
Exp. 3.9: ASTM Sensitivity Test for 13C NMR Spectroscopy 73
Exp. 3.10: Sensitivity Test for 13C NMR Spectroscopy 76
Exp. 3.11: Quadrature Image Test 79
Exp. 3.12: Dynamic Range Test for Signal Amplitudes 82
Exp. 3.13: 13° Phase Stability Test 85
Exp. 3.14: Radiofrequency Field Homogeneity 88
Chapter 4 Decoupling Techniques 91
Exp. 4.1: Decoupler Calibration for Homonuclear Decoupling 92
Exp. 4.2: Decoupler Calibration for Heteronuclear Decoupling 95
Exp. 4.3: Low-Power Calibration for Heteronuclear Decoupling 98
Exp. 4.4: Homonuclear Decoupling 101
Exp. 4.5: Homonuclear Decoupling at Two Frequencies 104
Exp. 4.6: The Homonuclear SPT Experiment 107
Exp. 4.7: The Heteronuclear SPT Experiment 110
Exp. 4.8: The Basic Homonuclear NOE Difference Experiment 113
Exp. 4.9: 1D Nuclear Overhauser Difference Spectroscopy 116
Exp. 4.10: 1D NOE Spectroscopy with Multiple Selective Irradiation 119
Exp. 4.11: 1H Off-Resonance Decoupled 13C NMR Spectra 122
Exp. 4.12: The Gated 1H-Decoupling Technique 125
Exp. 4.13: The Inverse Gated 1H-Decoupling Technique 128
Exp. 4.14: 1H Single-Frequency Decoupling of 13C NMR Spectra 131
Exp. 4.15: 1H Low-Power Decoupling of 13C NMR Spectra 134
Exp. 4.16: Measurement of the Heteronuclear Overhauser Effect 137
Chapter 5 Dynamic NMR Spectroscopy 140
Exp. 5.1: Low-Temperature Calibration Using Methanol 141
Exp. 5.2: High-Temperature Calibration Using 1,2-Ethanediol 145
Exp. 5.3: Dynamic 1H NMR Spectroscopy on Dimethylformamide 149
Exp. 5.4: The Saturation Transfer Experiment 152
Exp. 5.5: Measurement of the Rotating-Frame Relaxation Time T1¿ 155
Chapter 6 1D Multipulse Sequences 159
Exp. 6.1: Measurement of the Spin¿Lattice Relaxation Time T1 160
Exp. 6.2: Measurement of the Spin¿Spin Relaxation Time T2 164
Exp. 6.3: 13C NMR Spectra with SEFT 167
Exp. 6.4: 13C NMR Spectra with APT 170
Exp. 6.5: The Basic INEPT Technique 173
Exp. 6.6: INEPT+ 176
Exp. 6.7: Refocused INEPT 179
Exp. 6.8: Reverse INEPT 182
Exp. 6.9: DEPT-135 185
Exp. 6.10: Editing 13C NMR Spectra Using DEPT 188
Exp. 6.11: DEPTQ 191
Exp. 6.12: Multiplicity Determination Using PENDANT 194
Exp. 6.13: 1D-INADEQUATE 197
Exp. 6.14: The BIRD Filter 201
Exp. 6.15: TANGO 204
Exp. 6.16: The Heteronuclear Double-Quantum Filter 207
Exp. 6.17: Purging with a Spin-Lock Pulse 210
Exp. 6.18: Water Suppression by Presaturation 213
Exp. 6.19: Water Suppression by the Jump-and-Return Method 216
Chapter 7 NMR Spectroscopy with Selective Pulses 219
Exp. 7.1: Determination of a Shaped 90° 1H Transmitter Pulse 220
Exp. 7.2: Determination of a Shaped 90° 1H Decoupler Pulse 223
Exp. 7.3: Determination of a Shaped 90° 13C Decoupler Pulse 226
Exp. 7.4: Selective Excitation Using DANTE 229
Exp. 7.5: SELCOSY 232
Exp. 7.6: SELINCOR: Selective Inverse H,C Correlation via 1J(C,H) 235
Exp. 7.7: SELINQUATE 238
Exp. 7.8: Selective TOCSY 242
Exp. 7.9: INAPT 246
Exp. 7.10: Determination of Long-Range C,H Coupling Constants 249
Exp. 7.11: SELRESOLV 252
Exp. 7.12: SERF 255
Chapter 8 Auxiliary Reagents, Quantitative Determinations, and Reaction Mechanisms 258
Exp. 8.1: Signal Separation Using a Lanthanide Shift Reagent 259
Exp. 8.2: Signal Separation of Enantiomers Using a Chiral Shift Reagent 262
Exp. 8.3: Signal Separation of Enantiomers Using a Chiral Solvating Agent 265
Exp. 8.4: Determination of Enantiomeric Purity with Pirkle's Reagent 268
Exp. 8.5: Determination of Enantiomeric Purity by 31P NMR 271
Exp. 8.6: Determination of Absolute Configuration by the Advanced Mosher Method 274
Exp. 8.7: Aromatic Solvent-Induced Shift (ASIS) 277
Exp. 8.8: NMR Spectroscopy of OH Protons and H/D Exchange 280
Exp. 8.9: Water Suppression Using an Exchange Reagent 283
Exp. 8.10: Isotope Effects on Chemical Shielding 286
Exp. 8.11: pKa Determination by 13C NMR 290
Exp. 8.12: Determination of Association Constants Ka 293
Exp. 8.13: Saturation Transfer Difference NMR 298
Exp. 8.14: The Relaxation Reagent Cr(acac)3 302
Exp. 8.15: Determination of Paramagnetic Susceptibility by NMR 305
Exp. 8.16: 1H and 13C NMR of Paramagnetic Compounds 308
Exp. 8.17: The CIDNP Effect 312
Exp. 8.18: Quantitative 1H NMR Spectroscopy: Determination of the Alcohol Content of Polish Vodka 315
Exp. 8.19: Quantitative 13C NMR Spectroscopy with Inverse Gated 1H-Decoupling 318
Exp. 8.20: NMR Using Liquid-Crystal Solvents 321
Chapter 9 Heteronuclear NMR Spectroscopy 324
Exp. 9.1: 1H-Decoupled 15N NMR Spectra Using DEPT 330
Exp. 9.2: 1H-Coupled 15N NMR Spectra Using DEPT 333
Exp. 9.3: 19F NMR Spectroscopy 336
Exp. 9.4: 29Si NMR Spectroscopy Using DEPT 339
Exp. 9.5: 29Si NMR Spectroscopy Using Spin-Lock Polarization 342
Exp. 9.6: 119Sn NMR Spectroscopy 346
Exp. 9.7: 2H NMR Spectroscopy 349
Exp. 9.8: 11B NMR Spectroscopy 352
Exp. 9.9: 17O NMR Spectroscopy Using RIDE 355
Exp. 9.10: 47/49Ti NMR Spectroscopy Using ARING 358
Chapter 10 The Second Dimension 362
Exp. 10.1: 2D J-Resolved 1H NMR Spectroscopy 367
Exp. 10.2: 2D J-Resolved 13C NMR Spectroscopy 370
Exp. 10.3: The Basic H,H-COSY Experiment 373
Exp. 10.4: Long-Range COSY 377
Exp. 10.5: Phase-Sensitive COSY 380
Exp. 10.6: Phase-Sensitive COSY-45 383
Exp. 10.7: [...] 386
Exp. 10.8: Double-Quantum-Filtered COSY with Presaturation 389
Exp. 10.9: Fully Coupled C,H Correlation (FUCOUP) 393
Exp. 10.10: C,H-Correlation by Polarization Transfer (HETCOR) 396
Exp. 10.11: Long-Range C,H-Correlation by Polarization Transfer 399
Exp. 10.12: C,H Correlation via Long-Range Couplings (COLOC) 402
Exp. 10.13: The Basic HMQC Experiment 405
Exp. 10.14: Phase-Sensitive HMQC with BIRD Filter and GARP Decoupling 409
Exp. 10.15: Poor Man's Gradient HMQC 412
Exp. 10.16: Phase-Sensitive HMBC with BIRD Filter 415
Exp. 10.17: The Basic HSQC Experiment 418
Exp. 10.18: The HOHAHA or TOCSY Experiment 422
Exp. 10.19: HETLOC 426
Exp. 10.20: The NOESY Experiment 430
Exp. 10.21: The CAMELSPIN or ROESY Experiment 434
Exp. 10.22: The HOESY Experiment 438
Exp. 10.23: 2D-INADEQUATE 441
Exp. 10.24: The EXSY Experiment 445
Exp. 10.25: X,Y-Correlation 448
Chapter 11 1D NMR Spectroscopy with Pulsed Field Gradients 453
Exp. 11.1: Calibration of Pulsed Field Gradients 455
Exp. 11.2: Gradient Pre-emphasis 458
Exp. 11.3: Gradient Amplifier Test 461
Exp. 11.4: Determination of Pulsed Field Gradient Ring-Down Delays 464
Exp. 11.5: The Pulsed Field Gradient Spin-Echo Experiment 467
Exp. 11.6: Excitation Pattern of Selective Pulses 470
Exp. 11.7: The Gradient Heteronuclear Double-Quantum Filter 474
Exp. 11.8: The Gradient zz-Filter 477
Exp. 11.9: The Gradient-Selected Dual Step Low-Pass Filter 480
Exp. 11.10: gs-SELCOSY 484
Exp. 11.11: gs-SELTOCSY 488
Exp. 11.12: DPFGSE-NOE 492
Exp. 11.13: gs-SELINCOR 496
Exp. 11.14: ¿/ß-SELINCOR-TOCSY 499
Exp. 11.15: GRECCO 503
Exp. 11.16: WATERGATE 506
Exp. 11.17: Water Suppression by Excitation Sculpting 509
Exp. 11.18: Solvent Suppression Using WET 512
Exp. 11.19: DOSY 515
Exp. 11.20: INEPT-DOSY 518
Exp. 11.21: DOSY-HMQC 521
Chapter 12 2D NMR Spectroscopy With Field Gradients 525
Exp. 12.1: gs-COSY 526
Exp. 12.2: Constant-Time COSY 530
Exp. 12.3: Phase-Sensitive gs-DQF-COSY 534
Exp. 12.4: gs-HMQC 538
Exp. 12.5: gs-HMBC 542
Exp. 12.6: ACCORD-HMBC 546
Exp. 12.7: HMSC 550
Exp. 12.8: Phase-Sensititive gs-HSQC with Sensitivity Enhancement 554
Exp. 12.9: Edited HSQC with Sensitivity Enhancement 558
Exp. 12.10: HSQC with...
| Erscheinungsjahr: | 2004 |
|---|---|
| Fachbereich: | Chirurgie |
| Genre: | Mathematik, Medizin, Naturwissenschaften, Technik |
| Rubrik: | Wissenschaften |
| Medium: | Taschenbuch |
| Inhalt: |
XVI
838 S. 468 s/w Illustr. 10 s/w Tab. 478 Illustr. |
| ISBN-13: | 9783527310678 |
| ISBN-10: | 3527310673 |
| Sprache: | Englisch |
| Herstellernummer: | 1131067 000 |
| Einband: | Kartoniert / Broschiert |
| Autor: |
Berger, Stefan
Braun, Siegmar |
| Auflage: | 2nd expanded edition, reprinted |
| Hersteller: | Wiley-VCH GmbH |
| Verantwortliche Person für die EU: | Wiley-VCH GmbH, Boschstr. 12, D-69469 Weinheim, product-safety@wiley.com |
| Abbildungen: | 200 illus., 50 tabs. |
| Maße: | 244 x 170 x 45 mm |
| Von/Mit: | Stefan Berger (u. a.) |
| Erscheinungsdatum: | 11.05.2004 |
| Gewicht: | 1,635 kg |
Stefan Berger was intrigued by NMR after having won a bottle of beer during an introductory course in organic NMR led by Professor H. Suhr at the University of Tübingen in 1968. After completing a PhD thesis with Professor Anton Rieker, in 1973 he joined Professor J. D. Roberts at Caltech for postdoctoral work, where he also met Professor D.M. Grant and Professor D. Seebach, who were then guest professors in Pasadena. This period was decisive to try a Habilitation in NMR spectroscopy, which was achieved at the University Marburg. At the University Leipzig his aim is to combine methodological development of NMR and its application to bioorganic problems.
Preface v
Chapter 1 The NMR Spectrometer 1
1.1 Components of an NMR Spectrometer 1
1.1.1 The Magnet 1
1.1.2 The Spectrometer Cabinet 2
1.1.3 The Computer 3
1.1.4 Maintenance 3
1.2 Tuning a Probe-Head 3
1.3 The Lock Channel 4
1.4 The Art of Shimming 6
1.4.1 The Shim Gradients 6
1.4.2 The Shimming Procedure 8
1.4.3 Gradient Shimming 11
Chapter 2 Determination of Pulse-Duration 14
Exp. 2.1: Determination of the 90° 1H Transmitter Pulse-Duration 15
Exp. 2.2: Determination of the 90° 13C Transmitter Pulse-Duration 18
Exp. 2.3: Determination of the 90° 1H Decoupler Pulse-Duration 21
Exp. 2.4: The 90° 1H Pulse with Inverse Spectrometer Configuration 24
Exp. 2.5: The 90° 13C Decoupler Pulse with Inverse Configuration 27
Exp. 2.6: Composite Pulses 30
Exp. 2.7: Radiation Damping 33
Exp. 2.8: Pulse and Receiver Phases 36
Exp. 2.9: Determination of Radiofrequency Power 39
Chapter 3 Routine NMR Spectroscopy and Standard Tests 43
Exp. 3.1: The Standard 1H NMR Experiment 44
Exp. 3.2: The Standard 13C NMR Experiment 49
Exp. 3.3: The Application of Window Functions 54
Exp. 3.4: Computer-Aided Spectral Analysis 58
Exp. 3.5: Line Shape Test for 1H NMR Spectroscopy 61
Exp. 3.6: Resolution Test for 1H NMR Spectroscopy 64
Exp. 3.7: Sensitivity Test for 1H NMR Spectroscopy 67
Exp. 3.8: Line Shape Test for 13C NMR Spectroscopy 70
Exp. 3.9: ASTM Sensitivity Test for 13C NMR Spectroscopy 73
Exp. 3.10: Sensitivity Test for 13C NMR Spectroscopy 76
Exp. 3.11: Quadrature Image Test 79
Exp. 3.12: Dynamic Range Test for Signal Amplitudes 82
Exp. 3.13: 13° Phase Stability Test 85
Exp. 3.14: Radiofrequency Field Homogeneity 88
Chapter 4 Decoupling Techniques 91
Exp. 4.1: Decoupler Calibration for Homonuclear Decoupling 92
Exp. 4.2: Decoupler Calibration for Heteronuclear Decoupling 95
Exp. 4.3: Low-Power Calibration for Heteronuclear Decoupling 98
Exp. 4.4: Homonuclear Decoupling 101
Exp. 4.5: Homonuclear Decoupling at Two Frequencies 104
Exp. 4.6: The Homonuclear SPT Experiment 107
Exp. 4.7: The Heteronuclear SPT Experiment 110
Exp. 4.8: The Basic Homonuclear NOE Difference Experiment 113
Exp. 4.9: 1D Nuclear Overhauser Difference Spectroscopy 116
Exp. 4.10: 1D NOE Spectroscopy with Multiple Selective Irradiation 119
Exp. 4.11: 1H Off-Resonance Decoupled 13C NMR Spectra 122
Exp. 4.12: The Gated 1H-Decoupling Technique 125
Exp. 4.13: The Inverse Gated 1H-Decoupling Technique 128
Exp. 4.14: 1H Single-Frequency Decoupling of 13C NMR Spectra 131
Exp. 4.15: 1H Low-Power Decoupling of 13C NMR Spectra 134
Exp. 4.16: Measurement of the Heteronuclear Overhauser Effect 137
Chapter 5 Dynamic NMR Spectroscopy 140
Exp. 5.1: Low-Temperature Calibration Using Methanol 141
Exp. 5.2: High-Temperature Calibration Using 1,2-Ethanediol 145
Exp. 5.3: Dynamic 1H NMR Spectroscopy on Dimethylformamide 149
Exp. 5.4: The Saturation Transfer Experiment 152
Exp. 5.5: Measurement of the Rotating-Frame Relaxation Time T1¿ 155
Chapter 6 1D Multipulse Sequences 159
Exp. 6.1: Measurement of the Spin¿Lattice Relaxation Time T1 160
Exp. 6.2: Measurement of the Spin¿Spin Relaxation Time T2 164
Exp. 6.3: 13C NMR Spectra with SEFT 167
Exp. 6.4: 13C NMR Spectra with APT 170
Exp. 6.5: The Basic INEPT Technique 173
Exp. 6.6: INEPT+ 176
Exp. 6.7: Refocused INEPT 179
Exp. 6.8: Reverse INEPT 182
Exp. 6.9: DEPT-135 185
Exp. 6.10: Editing 13C NMR Spectra Using DEPT 188
Exp. 6.11: DEPTQ 191
Exp. 6.12: Multiplicity Determination Using PENDANT 194
Exp. 6.13: 1D-INADEQUATE 197
Exp. 6.14: The BIRD Filter 201
Exp. 6.15: TANGO 204
Exp. 6.16: The Heteronuclear Double-Quantum Filter 207
Exp. 6.17: Purging with a Spin-Lock Pulse 210
Exp. 6.18: Water Suppression by Presaturation 213
Exp. 6.19: Water Suppression by the Jump-and-Return Method 216
Chapter 7 NMR Spectroscopy with Selective Pulses 219
Exp. 7.1: Determination of a Shaped 90° 1H Transmitter Pulse 220
Exp. 7.2: Determination of a Shaped 90° 1H Decoupler Pulse 223
Exp. 7.3: Determination of a Shaped 90° 13C Decoupler Pulse 226
Exp. 7.4: Selective Excitation Using DANTE 229
Exp. 7.5: SELCOSY 232
Exp. 7.6: SELINCOR: Selective Inverse H,C Correlation via 1J(C,H) 235
Exp. 7.7: SELINQUATE 238
Exp. 7.8: Selective TOCSY 242
Exp. 7.9: INAPT 246
Exp. 7.10: Determination of Long-Range C,H Coupling Constants 249
Exp. 7.11: SELRESOLV 252
Exp. 7.12: SERF 255
Chapter 8 Auxiliary Reagents, Quantitative Determinations, and Reaction Mechanisms 258
Exp. 8.1: Signal Separation Using a Lanthanide Shift Reagent 259
Exp. 8.2: Signal Separation of Enantiomers Using a Chiral Shift Reagent 262
Exp. 8.3: Signal Separation of Enantiomers Using a Chiral Solvating Agent 265
Exp. 8.4: Determination of Enantiomeric Purity with Pirkle's Reagent 268
Exp. 8.5: Determination of Enantiomeric Purity by 31P NMR 271
Exp. 8.6: Determination of Absolute Configuration by the Advanced Mosher Method 274
Exp. 8.7: Aromatic Solvent-Induced Shift (ASIS) 277
Exp. 8.8: NMR Spectroscopy of OH Protons and H/D Exchange 280
Exp. 8.9: Water Suppression Using an Exchange Reagent 283
Exp. 8.10: Isotope Effects on Chemical Shielding 286
Exp. 8.11: pKa Determination by 13C NMR 290
Exp. 8.12: Determination of Association Constants Ka 293
Exp. 8.13: Saturation Transfer Difference NMR 298
Exp. 8.14: The Relaxation Reagent Cr(acac)3 302
Exp. 8.15: Determination of Paramagnetic Susceptibility by NMR 305
Exp. 8.16: 1H and 13C NMR of Paramagnetic Compounds 308
Exp. 8.17: The CIDNP Effect 312
Exp. 8.18: Quantitative 1H NMR Spectroscopy: Determination of the Alcohol Content of Polish Vodka 315
Exp. 8.19: Quantitative 13C NMR Spectroscopy with Inverse Gated 1H-Decoupling 318
Exp. 8.20: NMR Using Liquid-Crystal Solvents 321
Chapter 9 Heteronuclear NMR Spectroscopy 324
Exp. 9.1: 1H-Decoupled 15N NMR Spectra Using DEPT 330
Exp. 9.2: 1H-Coupled 15N NMR Spectra Using DEPT 333
Exp. 9.3: 19F NMR Spectroscopy 336
Exp. 9.4: 29Si NMR Spectroscopy Using DEPT 339
Exp. 9.5: 29Si NMR Spectroscopy Using Spin-Lock Polarization 342
Exp. 9.6: 119Sn NMR Spectroscopy 346
Exp. 9.7: 2H NMR Spectroscopy 349
Exp. 9.8: 11B NMR Spectroscopy 352
Exp. 9.9: 17O NMR Spectroscopy Using RIDE 355
Exp. 9.10: 47/49Ti NMR Spectroscopy Using ARING 358
Chapter 10 The Second Dimension 362
Exp. 10.1: 2D J-Resolved 1H NMR Spectroscopy 367
Exp. 10.2: 2D J-Resolved 13C NMR Spectroscopy 370
Exp. 10.3: The Basic H,H-COSY Experiment 373
Exp. 10.4: Long-Range COSY 377
Exp. 10.5: Phase-Sensitive COSY 380
Exp. 10.6: Phase-Sensitive COSY-45 383
Exp. 10.7: [...] 386
Exp. 10.8: Double-Quantum-Filtered COSY with Presaturation 389
Exp. 10.9: Fully Coupled C,H Correlation (FUCOUP) 393
Exp. 10.10: C,H-Correlation by Polarization Transfer (HETCOR) 396
Exp. 10.11: Long-Range C,H-Correlation by Polarization Transfer 399
Exp. 10.12: C,H Correlation via Long-Range Couplings (COLOC) 402
Exp. 10.13: The Basic HMQC Experiment 405
Exp. 10.14: Phase-Sensitive HMQC with BIRD Filter and GARP Decoupling 409
Exp. 10.15: Poor Man's Gradient HMQC 412
Exp. 10.16: Phase-Sensitive HMBC with BIRD Filter 415
Exp. 10.17: The Basic HSQC Experiment 418
Exp. 10.18: The HOHAHA or TOCSY Experiment 422
Exp. 10.19: HETLOC 426
Exp. 10.20: The NOESY Experiment 430
Exp. 10.21: The CAMELSPIN or ROESY Experiment 434
Exp. 10.22: The HOESY Experiment 438
Exp. 10.23: 2D-INADEQUATE 441
Exp. 10.24: The EXSY Experiment 445
Exp. 10.25: X,Y-Correlation 448
Chapter 11 1D NMR Spectroscopy with Pulsed Field Gradients 453
Exp. 11.1: Calibration of Pulsed Field Gradients 455
Exp. 11.2: Gradient Pre-emphasis 458
Exp. 11.3: Gradient Amplifier Test 461
Exp. 11.4: Determination of Pulsed Field Gradient Ring-Down Delays 464
Exp. 11.5: The Pulsed Field Gradient Spin-Echo Experiment 467
Exp. 11.6: Excitation Pattern of Selective Pulses 470
Exp. 11.7: The Gradient Heteronuclear Double-Quantum Filter 474
Exp. 11.8: The Gradient zz-Filter 477
Exp. 11.9: The Gradient-Selected Dual Step Low-Pass Filter 480
Exp. 11.10: gs-SELCOSY 484
Exp. 11.11: gs-SELTOCSY 488
Exp. 11.12: DPFGSE-NOE 492
Exp. 11.13: gs-SELINCOR 496
Exp. 11.14: ¿/ß-SELINCOR-TOCSY 499
Exp. 11.15: GRECCO 503
Exp. 11.16: WATERGATE 506
Exp. 11.17: Water Suppression by Excitation Sculpting 509
Exp. 11.18: Solvent Suppression Using WET 512
Exp. 11.19: DOSY 515
Exp. 11.20: INEPT-DOSY 518
Exp. 11.21: DOSY-HMQC 521
Chapter 12 2D NMR Spectroscopy With Field Gradients 525
Exp. 12.1: gs-COSY 526
Exp. 12.2: Constant-Time COSY 530
Exp. 12.3: Phase-Sensitive gs-DQF-COSY 534
Exp. 12.4: gs-HMQC 538
Exp. 12.5: gs-HMBC 542
Exp. 12.6: ACCORD-HMBC 546
Exp. 12.7: HMSC 550
Exp. 12.8: Phase-Sensititive gs-HSQC with Sensitivity Enhancement 554
Exp. 12.9: Edited HSQC with Sensitivity Enhancement 558
Exp. 12.10: HSQC with...
| Erscheinungsjahr: | 2004 |
|---|---|
| Fachbereich: | Chirurgie |
| Genre: | Mathematik, Medizin, Naturwissenschaften, Technik |
| Rubrik: | Wissenschaften |
| Medium: | Taschenbuch |
| Inhalt: |
XVI
838 S. 468 s/w Illustr. 10 s/w Tab. 478 Illustr. |
| ISBN-13: | 9783527310678 |
| ISBN-10: | 3527310673 |
| Sprache: | Englisch |
| Herstellernummer: | 1131067 000 |
| Einband: | Kartoniert / Broschiert |
| Autor: |
Berger, Stefan
Braun, Siegmar |
| Auflage: | 2nd expanded edition, reprinted |
| Hersteller: | Wiley-VCH GmbH |
| Verantwortliche Person für die EU: | Wiley-VCH GmbH, Boschstr. 12, D-69469 Weinheim, product-safety@wiley.com |
| Abbildungen: | 200 illus., 50 tabs. |
| Maße: | 244 x 170 x 45 mm |
| Von/Mit: | Stefan Berger (u. a.) |
| Erscheinungsdatum: | 11.05.2004 |
| Gewicht: | 1,635 kg |
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