200 and More NMR Experiments: A Practical Course

This work-book will guide you safely, in step-by-step descriptions, through every detail of the NMR experiments within, beginning with 1D routine experiments and ending with a series of advanced 3D experiments on a protein: ? 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

Table of Contents:
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 T1ρ 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: E.COSY 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: α/β-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 Adiabatic Pulses for High-Field Instruments 563 Exp. 12.11: gs-TOCSY 567 Exp. 12.12: gs-HMQC-TOCSY 571 Exp. 12.13: gs-HETLOC 575 Exp. 12.14: gs-J-Resolved HMBC 581 Exp. 12.15: 2Q-HMBC 585 Exp. 12.16: 1H-Detected 2D INEPT-INADEQUATE 589 Exp. 12.17: 1,1-ADEQUATE 593 Exp. 12.18: 1,n-ADEQUATE 597 Exp. 12.19: gs-NOESY 601 Exp. 12.20: gs-HSQC-NOESY 604 Exp. 12.21: gs-HOESY 608 Exp. 12.22: 1H,15N Correlation with gs-HMQC 612 Chapter 13 The Third Dimension 616 Exp. 13.1: 3D HMQC-COSY 618 Exp. 13.2: 3D gs-HSQC-TOCSY 622 Exp. 13.3: 3D H,C,P-Correlation 626 Exp. 13.4: 3D HMBC 630 Chapter 14 Solid-State NMR Spectroscopy 634 Exp. 14.1: Shimming Solid-State Probe-Heads 635 Exp. 14.2: Adjusting the Magic Angle 639 Exp. 14.3: Hartmann−Hahn Matching 642 Exp. 14.4: The Basic CP/MAS Experiment 645 Exp. 14.5: TOSS 649 Exp. 14.6: SELTICS 653 Exp. 14.7: Connectivity Determination in the Solid State 656 Exp. 14.8: REDOR 659 Exp. 14.9: High-Resolution Magic-Angle Spinning 663 Chapter 15 Protein NMR 666 Exp. 15.1: Pulse Determination for Protein NMR 670 Exp. 15.2: HN-HSQC 673 Exp. 15.3: HC-HSQC 678 Exp. 15.4: MUSIC 682 Exp. 15.5: HN-Correlation using TROSY 688 Exp. 15.6: HN-TOCSY-HSQC 692 Exp. 15.7: HNCA 698 Exp. 15.8: HN(CO)CA 705 Exp. 15.9: HNCO 711 Exp. 15.10: HN(CA)CO 718 Exp. 15.11: HCACO 725 Exp. 15.12: HCCH-TOCSY 732 Exp. 15.13: CBCANH 739 Exp. 15.14: CBCA(CO)NH 746 Exp. 15.15: HBHA(CBCACO)NH 753 Exp. 15.16: HN(CA)NNH 760 Exp. 15.17: HN-NOESY-HSQC 766 Exp. 15.18: HC-NOESY-HSQC 773 Exp. 15.19: 3D HCN-NOESY 779 Exp. 15.20: HNCA-J 785 Appendix 1 791 Pulse Programs Appendix 2 794 Instrument Dialects Appendix 3 797 Classification of Experiments Appendix 4 799 Elementary Product Operator Formalism Rules Appendix 5 802 Chemical Shift and Spin-Coupling Data for Ethyl Crotonate and Strychnine Glossary and Index 804

About the Author :
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.

Review :
"This book is an excellent catalogue of useful NMR experiments for people who are looking for the most suitable experiment to solve a specific problem. It collects in one place all the currently pulse sequences from liquid NMR spectroscopy, discusses their relative merits, the time required to perform them and gives experimental examples measured by the authors for this book. ... In conclusion, I think this book is a great encyclopedia of the techniques of modern liquid state NMR spectroscopy. It is highly readabele and should be on the shelf of any serious NMR spectroscopist, who does more complicated experiments than routine H-NMR spectroscopy. Finally instrument vendors should consider packing at least one copy of this book with every new NMR machine and using it as an educational toot when installing the machine." Dr. Gerd Buntkowsky, FSU Jena, Zeitschrift fur Physikalische Chemie, Band 218, Heft 11 "This third edition serves as a detailed guide to NMR, complete with 206 experiments ranging form 1-D trials to more complex 3-D experiments on proteins." Analytical Chemistry, November 1, 2004 "The handbook is written by experts and gives very detailed step-by-step instructions. ... This excellent book is very well written and builds on the success of the earlier version that was largely due to its clarity, information content and the fact that the methods worked." J. Lindon, Chromatographia 2005, Vol. 61/No. 1/2 "I highly recommend this book to all scientists who are trying to implement new experimental schemes in liquid-state NMR spectroscopy. It is a very useful NMR >cookbook< and a good starting point to find additional detailed information about experimental methods." Dr. Matthias Ernst, ETH Zurich, Physical Chemistry, ChemPhysChem, 5/2005 "...I find it to be one of the most useful books on my shelf...each new edition has brought substantial improvements...you will not be sorry if you acquire a copy for your personal library." Applied Spectroscopy, May 2005 "Beginnend von den >Basics< ...gelingt es den Autoren sehr schnell in die hochmoderne NMR-Technik einzusteigen. Dabei werden die wichtigsten der modernsten NMR-Methoden sehr gut und ausgiebig erklärt." www.chemieonline.de