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200 and More NMR Experiments

ISBN: 978-3-527-31067-8
854 pages
July 2004
200 and More NMR Experiments (3527310673) cover image
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
See More
Preface.

Chapter 1: The NMR Spectrometer.

1.1 Components of an NMR Spectrometer.

1.1.1 The Magnet.

1.1.2 The Spectrometer Cabinet.

1.1.3 The Computer.

1.1.4 Maintenance.

1.2 Tuning a Probe-Head.

1.3 The Lock Channel.

1.4 The Art of Shimming.

1.4.1 The Shim Gradients.

1.4.2 The Shimming Procedure.

1.4.3 Gradient Shimming.

Chapter 2: Determination of Pulse-Duration.

Exp. 2.1: Determination of the 90° 1H Transmitter Pulse-Duration.

Exp. 2.2: Determination of the 90° 13C Transmitter Pulse-Duration.

Exp. 2.3: Determination of the 90° 1H Decoupler Pulse-Duration.

Exp. 2.4: The 90° 1H Pulse with Inverse Spectrometer Configuration.

Exp. 2.5: The 90° 13C Decoupler Pulse with Inverse Configuration.

Exp. 2.6: Composite Pulses.

Exp. 2.7: Radiation Damping.

Exp. 2.8: Pulse and Receiver Phases.

Exp. 2.9: Determination of Radiofrequency Power.

Chapter 3: Routine NMR Spectroscopy and Standard Tests.

Exp. 3.1: The Standard 1H NMR Experiment.

Exp. 3.2: The Standard 13C NMR Experiment.

Exp. 3.3: The Application of Window Functions.

Exp. 3.4: Computer-Aided Spectral Analysis.

Exp. 3.5: Line Shape Test for 1H NMR Spectroscopy.

Exp. 3.6: Resolution Test for 1H NMR Spectroscopy.

Exp. 3.7: Sensitivity Test for 1H NMR Spectroscopy.

Exp. 3.8: Line Shape Test for 13C NMR Spectroscopy.

Exp. 3.9: ASTM Sensitivity Test for 13C NMR Spectroscopy.

Exp. 3.10: Sensitivity Test for 13C NMR Spectroscopy.

Exp. 3.11: Quadrature Image Test.

Exp. 3.12: Dynamic Range Test for Signal Amplitudes.

Exp. 3.13: 13° Phase Stability Test.

Exp. 3.14: Radiofrequency Field Homogeneity.

Chapter 4: Decoupling Techniques.

Exp. 4.1: Decoupler Calibration for Homonuclear Decoupling.

Exp. 4.2: Decoupler Calibration for Heteronuclear Decoupling.

Exp. 4.3: Low-Power Calibration for Heteronuclear Decoupling.

Exp. 4.4: Homonuclear Decoupling.

Exp. 4.5: Homonuclear Decoupling at Two Frequencies.

Exp. 4.6: The Homonuclear SPT Experiment.

Exp. 4.7: The Heteronuclear SPT Experiment.

Exp. 4.8: The Basic Homonuclear NOE Difference Experiment.

Exp. 4.9: 1D Nuclear Overhauser Difference Spectroscopy.

Exp. 4.10: 1D NOE Spectroscopy with Multiple Selective Irradiation.

Exp. 4.11: 1H Off-Resonance Decoupled 13C NMR Spectra.

Exp. 4.12: The Gated 1H-Decoupling Technique.

Exp. 4.13: The Inverse Gated 1H-Decoupling Technique.

Exp. 4.14: 1H Single-Frequency Decoupling of 13C NMR Spectra.

Exp. 4.15: 1H Low-Power Decoupling of 13C NMR Spectra.

Exp. 4.16: Measurement of the Heteronuclear Overhauser Effect.

Chapter 5: Dynamic NMR Spectroscopy.

Exp. 5.1: Low-Temperature Calibration Using Methanol.

Exp. 5.2: High-Temperature Calibration Using 1,2-Ethanediol.

Exp. 5.3: Dynamic 1H NMR Spectroscopy on Dimethylformamide.

Exp. 5.4: The Saturation Transfer Experiment.

Exp. 5.5: Measurement of the Rotating-Frame Relaxation Time T1ρ.

Chapter 6: 1D Multipulse Sequences.

Exp. 6.1: Measurement of the Spin−Lattice Relaxation Time T1.

Exp. 6.2: Measurement of the Spin−Spin Relaxation Time T2.

Exp. 6.3: 13C NMR Spectra with SEFT.

Exp. 6.4: 13C NMR Spectra with APT.

Exp. 6.5: The Basic INEPT Technique.

Exp. 6.6: INEPT+.

Exp. 6.7: Refocused INEPT.

Exp. 6.8: Reverse INEPT.

Exp. 6.9: DEPT-135.

Exp. 6.10: Editing 13C NMR Spectra Using DEPT.

Exp. 6.11: DEPTQ.

Exp. 6.12: Multiplicity Determination Using PENDANT.

Exp. 6.13: 1D-INADEQUATE.

Exp. 6.14: The BIRD Filter.

Exp. 6.15: TANGO.

Exp. 6.16: The Heteronuclear Double-Quantum Filter.

Exp. 6.17: Purging with a Spin-Lock Pulse.

Exp. 6.18: Water Suppression by Presaturation.

Exp. 6.19: Water Suppression by the Jump-and-Return Method.

Chapter 7: NMR Spectroscopy with Selective Pulses.

Exp. 7.1: Determination of a Shaped 90° 1H Transmitter Pulse.

Exp. 7.2: Determination of a Shaped 90° 1H Decoupler Pulse.

Exp. 7.3: Determination of a Shaped 90° 13C Decoupler Pulse.

Exp. 7.4: Selective Excitation Using DANTE.

Exp. 7.5: SELCOSY.

Exp. 7.6: SELINCOR: Selective Inverse H,C Correlation via 1J(C,H).

Exp. 7.7: SELINQUATE.

Exp. 7.8: Selective TOCSY.

Exp. 7.9: INAPT.

Exp. 7.10: Determination of Long-Range C,H Coupling Constants.

Exp. 7.11: SELRESOLV.

Exp. 7.12: SERF.

Chapter 8: Auxiliary Reagents, Quantitative Determinations, and Reaction Mechanisms.

Exp. 8.1: Signal Separation Using a Lanthanide Shift Reagent.

Exp. 8.2: Signal Separation of Enantiomers Using a Chiral Shift Reagent.

Exp. 8.3: Signal Separation of Enantiomers Using a Chiral Solvating Agent.

Exp. 8.4: Determination of Enantiomeric Purity with Pirkle’s Reagent.

Exp. 8.5: Determination of Enantiomeric Purity by 31P NMR.

Exp. 8.6: Determination of Absolute Configuration by the Advanced

Mosher Method.

Exp. 8.7: Aromatic Solvent-Induced Shift (ASIS).

Exp. 8.8: NMR Spectroscopy of OH Protons and H/D Exchange.

Exp. 8.9: Water Suppression Using an Exchange Reagent.

Exp. 8.10: Isotope Effects on Chemical Shielding.

Exp. 8.11: pKa Determination by 13C NMR.

Exp. 8.12: Determination of Association Constants Ka.

Exp. 8.13: Saturation Transfer Difference NMR.

Exp. 8.14: The Relaxation Reagent Cr(acac)3.

Exp. 8.15: Determination of Paramagnetic Susceptibility by NMR.

Exp. 8.16: 1H and 13C NMR of Paramagnetic Compounds.

Exp. 8.17: The CIDNP Effect.

Exp. 8.18: Quantitative 1H NMR Spectroscopy: Determination of the Alcohol Content of Polish Vodka.

Exp. 8.19: Quantitative 13C NMR Spectroscopy with Inverse Gated 1H-Decoupling.

Exp. 8.20: NMR Using Liquid-Crystal Solvents.

Chapter 9: Heteronuclear NMR Spectroscopy.

Exp. 9.1: 1H-Decoupled 15N NMR Spectra Using DEPT.

Exp. 9.2: 1H-Coupled 15N NMR Spectra Using DEPT.

Exp. 9.3: 19F NMR Spectroscopy.

Exp. 9.4: 29Si NMR Spectroscopy Using DEPT.

Exp. 9.5: 29Si NMR Spectroscopy Using Spin-Lock Polarization.

Exp. 9.6: 119Sn NMR Spectroscopy.

Exp. 9.7: 2H NMR Spectroscopy.

Exp. 9.8: 11B NMR Spectroscopy.

Exp. 9.9: 17O NMR Spectroscopy Using RIDE.

Exp. 9.10: 47/49Ti NMR Spectroscopy Using ARING.

Chapter 10: The Second Dimension.

Exp. 10.1: 2D J-Resolved 1H NMR Spectroscopy.

Exp. 10.2: 2D J-Resolved 13C NMR Spectroscopy.

Exp. 10.3: The Basic H,H-COSY Experiment.

Exp. 10.4: Long-Range COSY.

Exp. 10.5: Phase-Sensitive COSY.

Exp. 10.6: Phase-Sensitive COSY-45.

Exp. 10.7: E.COSY.

Exp. 10.8: Double-Quantum-Filtered COSY with Presaturation.

Exp. 10.9: Fully Coupled C,H Correlation (FUCOUP).

Exp. 10.10: C,H-Correlation by Polarization Transfer (HETCOR).

Exp. 10.11: Long-Range C,H-Correlation by Polarization Transfer.

Exp. 10.12: C,H Correlation via Long-Range Couplings (COLOC).

Exp. 10.13: The Basic HMQC Experiment.

Exp. 10.14: Phase-Sensitive HMQC with BIRD Filter and GARP Decoupling.

Exp. 10.15: Poor Man’s Gradient HMQC.

Exp. 10.16: Phase-Sensitive HMBC with BIRD Filter.

Exp. 10.17: The Basic HSQC Experiment.

Exp. 10.18: The HOHAHA or TOCSY Experiment.

Exp. 10.19: HETLOC.

Exp. 10.20: The NOESY Experiment.

Exp. 10.21: The CAMELSPIN or ROESY Experiment.

Exp. 10.22: The HOESY Experiment.

Exp. 10.23: 2D-INADEQUATE.

Exp. 10.24: The EXSY Experiment.

Exp. 10.25: X,Y-Correlation.

Chapter 11: 1D NMR Spectroscopy with Pulsed Field Gradients.

Exp. 11.1: Calibration of Pulsed Field Gradients.

Exp. 11.2: Gradient Pre-emphasis.

Exp. 11.3: Gradient Amplifier Test.

Exp. 11.4: Determination of Pulsed Field Gradient Ring-Down Delays.

Exp. 11.5: The Pulsed Field Gradient Spin-Echo Experiment.

Exp. 11.6: Excitation Pattern of Selective Pulses.

Exp. 11.7: The Gradient Heteronuclear Double-Quantum Filter.

Exp. 11.8: The Gradient zz-Filter.

Exp. 11.9: The Gradient-Selected Dual Step Low-Pass Filter.

Exp. 11.10: gs-SELCOSY.

Exp. 11.11: gs-SELTOCSY.

Exp. 11.12: DPFGSE-NOE.

Exp. 11.13: gs-SELINCOR.

Exp. 11.14: α/β-SELINCOR-TOCSY.

Exp. 11.15: GRECCO.

Exp. 11.16: WATERGATE.

Exp. 11.17: Water Suppression by Excitation Sculpting.

Exp. 11.18: Solvent Suppression Using WET.

Exp. 11.19: DOSY.

Exp. 11.20: INEPT-DOSY.

Exp. 11.21: DOSY-HMQC.

Chapter 12: 2D NMR Spectroscopy With Field Gradients.

Exp. 12.1: gs-COSY.

Exp. 12.2: Constant-Time COSY.

Exp. 12.3: Phase-Sensitive gs-DQF-COSY.

Exp. 12.4: gs-HMQC.

Exp. 12.5: gs-HMBC.

Exp. 12.6: ACCORD-HMBC.

Exp. 12.7: HMSC.

Exp. 12.8: Phase-Sensititive gs-HSQC with Sensitivity Enhancement.

Exp. 12.9: Edited HSQC with Sensitivity Enhancement.

Exp. 12.10: HSQC with Adiabatic Pulses for High-Field Instruments.

Exp. 12.11: gs-TOCSY.

Exp. 12.12: gs-HMQC-TOCSY.

Exp. 12.13: gs-HETLOC.

Exp. 12.14: gs-J-Resolved HMBC.

Exp. 12.15: 2Q-HMBC.

Exp. 12.16: 1H-Detected 2D INEPT-INADEQUATE.

Exp. 12.17: 1,1-ADEQUATE.

Exp. 12.18: 1,n-ADEQUATE.

Exp. 12.19: gs-NOESY.

Exp. 12.20: gs-HSQC-NOESY.

Exp. 12.21: gs-HOESY.

Exp. 12.22: 1H,15N Correlation with gs-HMQC.

Chapter 13: The Third Dimension.

Exp. 13.1: 3D HMQC-COSY.

Exp. 13.2: 3D gs-HSQC-TOCSY.

Exp. 13.3: 3D H,C,P-Correlation.

Exp. 13.4: 3D HMBC.

Chapter 14: Solid-State NMR Spectroscopy.

Exp. 14.1: Shimming Solid-State Probe-Heads.

Exp. 14.2: Adjusting the Magic Angle.

Exp. 14.3: Hartmann−Hahn Matching.

Exp. 14.4: The Basic CP/MAS Experiment.

Exp. 14.5: TOSS.

Exp. 14.6: SELTICS.

Exp. 14.7: Connectivity Determination in the Solid State.

Exp. 14.8: REDOR.

Exp. 14.9: High-Resolution Magic-Angle Spinning.

Chapter 15: Protein NMR.

Exp. 15.1: Pulse Determination for Protein NMR.

Exp. 15.2: HN-HSQC.

Exp. 15.3: HC-HSQC.

Exp. 15.4: MUSIC.

Exp. 15.5: HN-Correlation using TROSY.

Exp. 15.6: HN-TOCSY-HSQC.

Exp. 15.7: HNCA.

Exp. 15.8: HN(CO)CA.

Exp. 15.9: HNCO.

Exp. 15.10: HN(CA)CO.

Exp. 15.11: HCACO.

Exp. 15.12: HCCH-TOCSY.

Exp. 15.13: CBCANH.

Exp. 15.14: CBCA(CO)NH.

Exp. 15.15: HBHA(CBCACO)NH.

Exp. 15.16: HN(CA)NNH.

Exp. 15.17: HN-NOESY-HSQC.

Exp. 15.18: HC-NOESY-HSQC.

Exp. 15.19: 3D HCN-NOESY.

Exp. 15.20: HNCA-J.

Appendix 1: Pulse Programs.

Appendix 2: Instrument Dialects.

Appendix 3: Classification of Experiments.

Appendix 4: Elementary Product Operator Formalism Rules.

Appendix 5: Chemical Shift and Spin-Coupling Data for Ethyl Crotonate and Strychnine.

Glossary and Index.

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What is new in this third edition?
  • 24 new experiments have been inserted into the 14 chapters that were in the 2nd edition, e.g., α/β-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.
  • 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.
See More
  • 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?
  • The guide has been written by experts in this field, following the principle of learning by doing.
  • All experiments have been specially performed for this book, exactly as described and depicted, exactly as described and shown in the spectra that are reproduced.
  • Being a reference source and work-book forthe 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.
See More
"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 für 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 Zürich, 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




"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 für physikalische Chemie, Band 218, Heft 11

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