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 descr ibed 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.

Spis treści:
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 Tes t.
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 1