Webb Annual Reports on NMR Spectroscopy

1. Auflage 2014
ISBN: 978-0-12-800327-5
Verlag: Elsevier Science & Techn.
Format: EPUB
Kopierschutz: 6 - ePub Watermark

E-Book, Englisch, Band Volume 83, 376 Seiten

Reihe: Annual Reports on NMR Spectroscopy

Nuclear magnetic resonance (NMR) is an analytical tool used by chemists and physicists to study the structure and dynamics of molecules. In recent years, no other technique has gained such significance as NMR spectroscopy. It is used in all branches of science in which precise structural determination is required and in which the nature of interactions and reactions in solution is being studied. Annual Reports on NMR Spectroscopy has established itself as a premier means for the specialist and non-specialist alike to become familiar with new techniques and applications of NMR spectroscopy. - This volume of Annual Reports on NMR Spectroscopy focuses on the analytical tools used by chemists and physicists, taken together with other volumes of this series, an excellent account of progress in NMR and its many applications is provided and anyone using NMR will find interest in this Serial

Autoren/Hrsg.

Webb, Graham A.

Inhaltsverzeichnis

1;Front Cover;1
2;Annual Reports on NMR Spectroscopy;4
3;Copyright;5
4;Contents;6
5;Contributors;8
6;Preface;10
7;Chapter One: Dynamic Pictures of Proteins by NMR;12
7.1;1. Introduction;13
7.2;2. Pico- to Nanosecond Motions;15
7.2.1;2.1. Generalized Order Parameters from the Relaxation Parameters [8-10,30-33];16
7.2.2;2.2. Moiety of Membrane Proteins Protruding from Membrane Surfaces;20
7.3;3. Micro- to Milliseconds Motions: Solution NMR;22
7.3.1;3.1. CPMG R2 Relaxation Rate Dispersion;23
7.3.2;3.2. R1. Relaxation Rate Dispersion;27
7.3.3;3.3. Differential ZQC/DQC Decay Rates;30
7.3.4;3.4. ZZ-Exchange;30
7.3.5;3.5. Residual Dipolar Couplings;31
7.4;4. Micro- to Millisecond Motions: Solid State NMR;35
7.4.1;4.1. Dynamic Interference: SRI;35
7.4.2;4.2. CODEX and Chemical Exchange;38
7.4.3;4.3. Order Parameters Based on DCs;40
7.4.4;4.4. Relaxation Rate parameters: R1, R2, and R1.;41
7.4.5;4.5. Lineshape Analysis;45
7.5;5. Very Slow Motions: 1D MAS Exchange;46
7.6;6. Globular Proteins;48
7.6.1;6.1. Comparison of Protein Dynamics Between Solution and Solid;48
7.6.2;6.2. Pico- to Nanosecond motions: Conformational Entropy and Allostery;48
7.6.3;6.3. ms-µs Motions: Biological Function;51
7.6.3.1;6.3.1. Protein Folding;51
7.6.3.2;6.3.2. Catalysis and Allosteric Regulation;52
7.7;7. Membrane Proteins;54
7.7.1;7.1. Retinal Proteins;54
7.7.1.1;7.1.1. Bacteriorhodopsin (bR);54
7.7.1.2;7.1.2. Sensory Rhodopsin and Proteorhodopsin;58
7.7.2;7.2. Other Proteins;60
7.8;8. Conclusion;61
7.9;Acknowledgements;62
7.10;References;62
8;Chapter Two: Recent Progress in the Solid-State NMR Studies of Short Peptides: Techniques, Structure and Dynamics;78
8.1;1. Introduction;79
8.2;2. Development of the New Solid-State NMR Techniques Useful in Structural Studies of Peptides;81
8.2.1;2.1. 1H Solid-State NMR;81
8.2.2;2.2. 13C and 15N Sensitivity under Fast and Medium Magic-Angle Spinning;83
8.2.3;2.3. Two-Dimensional Correlations under F-MAS;89
8.2.3.1;2.3.1. 1H-13C and 1H-15N HETCOR Correlations;89
8.2.3.2;2.3.2. 13C-13C and 15N-15N HOMCOR Correlations;91
8.2.4;2.4. Quadrupolar Nuclei;93
8.3;3. Molecular Dynamics of Peptides in the Solid State;94
8.3.1;3.1. Probing the Dynamics in Different Time Scales;95
8.3.2;3.2. Tools for Analysis of the Local Molecular Motions of Peptides in the Solid State;98
8.3.2.1;3.2.1. Relaxation Times;98
8.3.2.2;3.2.2. Chemical Shift Anisotropy;102
8.3.2.3;3.2.3. Investigation of the Dynamics by Deuterium Solid-State NMR: Line-Shape Analysis;106
8.3.2.4;3.2.4. Heteronuclear Dipolar Recoupling Sequences;112
8.4;4. Polymorphism and Solvatomorphism of Peptides;116
8.4.1;4.1. Solid-State NMR Study of Polymorphs and Solvatomorphs;117
8.4.1.1;4.1.1. Ala-Ala-Ala Tripeptide-The Case Study;122
8.5;5. Complementarity of Theoretical and NMR Methods in Assignment of the Solid-State Structure of Peptides;126
8.5.1;5.1. Techniques Used for Calculations of NMR Parameters in the Solid State;129
8.5.2;5.2. Theoretical Methods as a Tool for Structure Assignment of Peptides in the Solid State;130
8.5.3;5.3. Fine Refinement of Peptide Crystals with Molecular Disorder;135
8.5.4;5.4. Theoretical Methods Versus Molecular Motion;140
8.6;6. Concluding Remarks;142
8.7;Acknowledgement;143
8.8;References;143
9;Chapter Three: Solid-State 17O NMR Studies of Biomolecules;156
9.1;1. Introduction;157
9.2;2. NMR Tensor Parameters;160
9.3;3. NMR Methodologies;163
9.3.1;3.1. Site-Specific Spectral Resolution;164
9.3.1.1;3.1.1. Single-Crystal NMR;164
9.3.1.2;3.1.2. Magic-Angle Spinning;165
9.3.1.3;3.1.3. MQMAS and STMAS;166
9.3.1.4;3.1.4. Dynamic Angle Spinning and Double Rotation;168
9.3.2;3.2. Detection Sensitivity Enhancement;169
9.3.2.1;3.2.1. Isotopic Enrichment and High Magnetic Field;169
9.3.2.2;3.2.2. Spin Population Transfer Experiments;170
9.3.2.3;3.2.3. Dynamic Nuclear Polarization;171
9.3.2.4;3.2.4. Cryo-MAS;172
9.3.2.5;3.2.5. Cross-polarization;173
9.3.3;3.3. Correlation NMR Experiments;174
9.3.4;3.4. Quantum Chemical Calculations;178
9.3.4.1;3.4.1. Molecular Cluster Model;179
9.3.4.2;3.4.2. Periodic Crystal Lattice;180
9.3.5;3.5. Basic NMR Experimental Considerations;180
9.3.6;3.6. General Schemes for Determining the Tensor Parameters;182
9.3.6.1;3.6.1. Single Oxygen;183
9.3.6.2;3.6.2. Multiple Oxygens;183
9.4;4. 17O NMR Studies of Biomolecules;186
9.4.1;4.1. Proteins;189
9.4.1.1;4.1.1. Amino Acids;189
9.4.1.2;4.1.2. Peptides;191
9.4.1.3;4.1.3. Proteins;195
9.4.2;4.2. Nucleic Acids;197
9.4.3;4.3. Carbohydrates;198
9.4.4;4.4. Recent Progress on Organic Molecules of Biological Relevance;201
9.4.4.1;4.4.1. Carboxylic Acids and Carboxylates;201
9.4.4.2;4.4.2. C-Nitroso Compounds;204
9.4.4.3;4.4.3. Keto Acids;204
9.4.4.4;4.4.4. Sulfonic Acids;205
9.5;5. Concluding Remarks;206
9.6;Acknowledgements;207
9.7;Appendix;208
9.8;References;224
10;Chapter Four: Solid-State Nuclear Magnetic Resonance in Pharmaceutical Compounds;232
10.1;1. Introduction;233
10.2;2. SSNMR Techniques;236
10.2.1;2.1. 1D High-Resolution SSNMR Experiments;236
10.2.1.1;2.1.1. Diluted Spins;236
10.2.1.2;2.1.2. High-Resolution 1H NMR MAS;238
10.2.2;2.2. 2D SSNMR Experiments;240
10.2.3;2.3. First Principles Calculations;241
10.2.4;2.4. Relaxation Time Measurements;241
10.2.5;2.5. Multinuclear SSNMR;242
10.3;3. SSNMR of Pharmaceutical Compounds;243
10.3.1;3.1. API Characterization;243
10.3.2;3.2. Polymorphism;248
10.3.3;3.3. Pharmaceutical Complexes with Cyclodextrins;257
10.3.4;3.4. Salts and Cocrystals;261
10.3.5;3.5. NMR Crystallography;267
10.3.6;3.6. Tablet Characterization;270
10.4;4. Conclusions;271
10.5;5. Table of Compounds;271
10.6;Acknowledgements;273
10.7;References;273
11;Chapter Five: Covariance NMR and Small Molecule Applications;282
11.1;1. Introduction;283
11.2;2. On the Theory of Covariance NMR;284
11.2.1;2.1. The General Description;284
11.2.2;2.2. Types of Covariance Transformations in NMR;289
11.2.2.1;2.2.1. The Classification of Covariance NMR;289
11.2.2.2;2.2.2. Some Aspects of the Workings of 4D NMR;291
11.2.2.3;2.2.3. Matrix Regularization in Covariance NMR;292
11.2.2.4;2.2.4. The Transition from Indirect to Unsymmetrical Indirect Covariance;292
11.2.2.5;2.2.5. The Workings of Generalized Indirect Covariance NMR;293
11.2.3;2.3. Examples of Covariance Transformations;295
11.2.4;2.4. Artefacts in Covariance NMR Spectra;300
11.2.5;2.5. The Determination of the Non-Linear Signal-to-Noise Ratio;301
11.2.6;2.6. Asynchronous Spectra-The Neglected Imaginary Part;302
11.2.6.1;2.6.1. General Aspects of Asynchronous Spectra;302
11.2.6.2;2.6.2. Applications of Asynchronous Spectra;304
11.2.7;2.7. Heterospectroscopy;305
11.3;3. Software for Covariance NMR Processing;307
11.4;4. Covariance and NUS-The Combination of Two Approaches to Fast Methods;311
11.5;5. Applications of Covariance NMR to Small Molecules;317
11.5.1;5.1. Direct Covariance;317
11.5.1.1;5.1.1. Solution State;317
11.5.1.2;5.1.2. Solid State;320
11.5.2;5.2. Indirect Covariance;321
11.5.2.1;5.2.1. Solution State;321
11.5.2.2;5.2.2. Solid State;327
11.5.3;5.3. Unsymmetrical and Generalized Indirect Covariance;329
11.5.4;5.4. Multidimensional Covariance;344
11.5.4.1;5.4.1. Triple Rank;344
11.5.4.2;5.4.2. 4D NMR;345
11.5.5;5.5. Synchronous and Asynchronous Spectra;346
11.5.6;5.6. Statistical Analysis of NMR Spectra in the Field of Metabolomics;347
11.5.7;5.7. Other Covariance Applications in NMR Spectroscopy;349
11.6;6. Conclusion;351
11.7;Acknowledgements;352
11.8;References;352
12;Index;362

Leseproben

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