Nuclear Magnetic Resonance Spectroscopy: An Introduction to Principles, Applications, and Experimental Methods

ISBN-13: 9781119295235 / Angielski / Twarda / 2019 / 480 str.

Joseph B. Lambert; Eugene Mazzola; Clark D. Ridge

Opis

Combines clear and concise discussions of key NMR concepts with succinct and illustrative examples

Designed to cover a full course in Nuclear Magnetic Resonance (NMR) Spectroscopy, this text offers complete coverage of classic (one–dimensional) NMR as well as up–to–date coverage of two–dimensional NMR and other modern methods.

Spis treści

Preface to First Edition

Preface to Second Edition

Symbols

Abbreviations

1. Introduction

1.1. Magnetic Properties of Nuclei

1.2. The Chemical Shift

1.3. Excitation and Relaxation

1.4. Pulsed Experiments

1.5. The Coupling Constant

1.6. Quantitation and Complex Splitting

1.7. Commonly Studied Nuclides

1.8. Dynamic Effects

1.9. Spectra of Solids

Problems

Tips on Solving NMR Problems

Bibliography

2. Introductory Experimental Methods

2.1. The Spectrometer

2.2. Sample Preparation

2.3. Optimizing the Signal

2.3a. Sample Tube Placement

2.3b. Probe Tuning

2.3c. Field/Frequency Locking

2.3d. Spectrometer Shimming

2.4. Determination of NMR Spectra–Acquisition Parameters

2.4a. Number of Data Points

2.4b. Spectral Width

2.4c. Filter Bandwidth

2.4d. Acquisition Time

2.4e. Transmitter Offset

2.4f. Flip Angle

2.4g. Receiver Gain

2.4h. Number of Scans

2.4i. Steady–State Scans

2.4j. Oversampling and Digital Filtration

2.4k. Decoupling for X Nuclei

2.4l. Typical NMR Experiments

2.5. Determination of NMR Spectral–Processing Parameters

2.5a. Exponential Weighting

2.5b. Zero Filling

2.5c. FID Truncation and Spectral Artifacts

2.5d. Resolution

2.6. Determination of NMR Spectra:  Spectral Presentation

2.6a. Signal Phasing and Baseline Correction

2.6b. Zero Referencing

2.6c. Determination of Certain NMR Parameters

2.7. Calibrations

2.7a. Pulse Width (Flip Angle)

2.8b. Decoupler Field Strength

Problems

Bibliography

3. The Chemical Shift

3.1. Factors That Influence Proton Shifts

3.2. Proton Chemical Shifts and Structure

3.2a. Saturated Aliphatics

3.2b. Unsaturated Aliphatics

3.2c. Aromatics

3.2d. Protons on Oxygen and Nitrogen

3.2e. Programs for Empirical Calculations

3.3. Medium and Isotope Effects

3.4. Factors That Influence Carbon Shifts

3.5. Carbon Chemical Shifts and Structure

3.5a. Saturated Aliphatics

3.5b. Unsaturated Compounds

3.5c. Carbonyl Groups

3.5d. Programs for Empirical Calculation

3.6. Tables of Chemical Shifts

Problems

Further Tips on Solving NMR Problems

Bibliography

4. The Coupling Constant

4.1. First– and Second–Order Effects

4.2. Chemical and Magnetic Equivalence

4.3. Signs and Mechanisms of Coupling

4.4. Couplings over One Bond

4.5. Geminal Couplings

4.6. Vicinal Couplings

4.7. Long–Range Couplings

4.8. Spectral Analysis

4.9. Tables of Coupling Constants

Problems

Bibliography

5. Further Topics in One–Dimensional NMR Spectroscopy

5.1. Spin–Lattice and Spin–Spin Relaxation

5.2. Reactions on the NMR Time Scale

5.3. Multiple Resonance

5.4. The Nuclear Overhauser Effect

5.5. Spectral Editing

5.6. Sensitivity Enhancement

5.7. Carbon Connectivity

5.8. Phase Cycling, Composite Pulses, and Shaped Pulses

Problems

Bibliography

6. Two–Dimensional NMR Spectroscopy

6.1. Proton–Proton Correlation Through J Coupling

6.2. Proton–Heteronucleus Correlation

6.3. Proton–Proton Correlation Through Space or Chemical Exchange

6.4. Carbon–Carbon Correlation

6.5. Higher Dimensions

6.6. Pulsed Field Gradients

6.7. Diffusion–Ordered Spectroscopy

6.7. Summary of Two–Dimensional Methods

Problems

Bibliography

7. Advanced Experimental Methods

Part A. One–Dimensional Techniques

7.1. T₁ Measurements

7.2. ¹³C Spectral Editing Experiments

7.2a. The APT Experiment

7.2b. The DEPT Experiment

7.3. NOE Experiments

7.3a. The NOE Difference Experiment

7.3b. The Double–Pulse, Field–Gradient, Spin–Echo NOE Experiment

Part B. Two–Dimensional Techniques

7.4. Two–Dimensional NMR Data–Acquisition Parameters

7.4a. Number of Data Points

7.4b. Number of Time Increments

7.4c. Spectral Widths

7.4d. Acquisition Time

7.4e. Transmitter Offset

7.4f. Flip Angle

7.4g. Relaxation Delay

7.4h. Receiver Gain

7.4i. Number of Scans per Time Increment

7.4j. Steady–State Scans

7.5. Two–Dimensional NMR Data–Processing Parameters

7.5a. Weighting Functions

7.5b. Zero Filling

7.5c. Digital Resolution

7.5d. Linear Prediction

7.6. Two–Dimensional NMR Data Display

7.6a. Phasing and Zero Referencing

7.6b. Symmetrization

7.6c. Use of Cross Sections in Analysis

Part C. Two–Dimensional Techniques:  The Experiments

7.7. Homonuclear Chemical–Shift Correlation Experiments via Scalar Coupling

7.7a. The COSY Family:  COSY–90°, COSY–45°, Long–Range COSY, and DQF–COSY

7.7b. The TOCSY Experiment

7.8. Direct Heteronuclear Chemical–Shift Correlation via Scalar Coupling

7.8a. The HMQC Experiment

7.8b. The HSQC Experiment

7.8c. The HETCOR Experiment

7.9. Indirect Heteronuclear Chemical–Shift Correlation via Scalar Coupling

7.9a. The HMBC Experiment

7.9b. The FLOCK Experiment

7.9c. The HSQC–TOCSY Experiment

7.10. Homonuclear Chemical–Shift Correlation via Dipolar Coupling

7.10a. The NOESY Experiment

7.10b. The ROESY Experiment

7.11. 1D and Advanced 2D Experiments

7.11a. The 1D TOCSY Experiment

7.11b. The 1D NOESY and ROESY Experiments

7.11c. The Multiplicity–Edited HSQC Experiment

7.11d. The H2BC Experiment

7.11e. Nonuniform Sampling

7.11f. Pure Shift NMR

7.11g. Covariance NMR

7.12. Pure Shift–Covariance NMR

Bibliography

8. Structural Elucidation:  An Example

Part A. Spectral Analysis

8.1. ¹H NMR Data

8.2. ¹³C NMR Data

8.3. The DEPT Experiment

8.4. The HSQC Experiment

8.5. The COSY Experiment

8.6. The HMBC Experiment

8.7. General Molecular Assembly Strategy

8.8. A Specific Molecular Assembly Procedure

8.9. The NOESY Experiment

Part B Computer–Assisted Structure Elucidation

8.10. CASE Procedures

8.11. T–2 Toxin

Appendix 1 Derivation of the NMR Equation

Appendix 2 The Bloch Equations

Appendix 3 Quantum Mechanical Treatment of the Two–Spin System

Appendix 4 Analysis of Second–Order, Three– and Four–Spin Systems by Inspection

Appendix 5 Relaxation

Appendix 6 Product–Operator Formalism and Coherence–Level Diagrams

Bibliography

Appendix 7 Stereochemical Considerations

A7.1. Homotopic Groups

A7.2. Enantiotopic Groups

A7.3. Diastereotopic Groups

Bibliography

Index

O autorze

Joseph B. Lambert, Ph.D., is Research Professor of Chemistry at Trinity University.

Eugene P. Mazzola, Ph.D., is an adjunct professor of chemistry at the University of Maryland as well as a researcher at the UMD FDA Joint Institute for Food Safety and Applied Nutrition.

Clark D. Ridge, Ph.D., is an NMR spectroscopist based at the Health and Human Sciences division of the FDA at College Park, Maryland.

Blurb

Combines clear and concise discussions of key NMR concepts with succinct and illustrative examples

Designed to cover a full course in Nuclear Magnetic Resonance (NMR) Spectroscopy, this text offers complete coverage of classic (one–dimensional) NMR as well as up–to–date coverage of two–dimensional NMR and other modern methods. It contains practical advice, theory, illustrated applications, and classroom–tested problems; looks at such important ideas as relaxation, NOEs, phase cycling, and processing parameters; and provides brief, yet fully comprehensible, examples. It also uniquely lists all of the general parameters for many experiments including mixing times, number of scans, relaxation times, and more.

Nuclear Magnetic Resonance Spectroscopy: An Introduction to Principles, Applications, and Experimental Methods, 2nd Edition begins by introducing readers to NMR spectroscopy – an analytical technique used in modern chemistry, biochemistry, and biology that allows identification and characterization of organic, and some inorganic, compounds. It offers chapters covering: Experimental Methods; The Chemical Shift; The Coupling Constant; Further Topics in One–Dimensional NMR Spectroscopy; Two–Dimensional NMR Spectroscopy; Advanced Experimental Methods; and Structural Elucidation.

• Features classical analysis of chemical shifts and coupling constants for both protons and other nuclei, as well as modern multi pulse and multi–dimensional methods
• Contains experimental procedures and practical advice relative to the execution of NMR experiments
• Includes a chapter–long, worked–out problem that illustrates the application of nearly all current methods
• Offers appendices containing the theoretical basis of NMR, including the most modern approach that uses product operators and coherence–level diagrams

By offering a balance between volumes aimed at NMR specialists and the structure–determination–only books that focus on synthetic organic chemists, Nuclear Magnetic Resonance Spectroscopy: An Introduction to Principles, Applications, and Experimental Methods, 2nd Edition is an excellent text for students and post–graduate students working in analytical and bio–sciences, as well as scientists who use NMR spectroscopy as a primary tool in their work.