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
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
Front Cover 1
Annual Reports on NMR Spectroscopy 4
Copyright 5
Contents 6
Contributors 8
Preface 10
Chapter One: Dynamic Pictures of Proteins by NMR 12
1. Introduction 13
2. Pico- to Nanosecond Motions 15
2.1. Generalized Order Parameters from the Relaxation Parameters [8-10,30-33] 16
2.2. Moiety of Membrane Proteins Protruding from Membrane Surfaces 20
3. Micro- to Milliseconds Motions: Solution NMR 22
3.1. CPMG R2 Relaxation Rate Dispersion 23
3.2. R1. Relaxation Rate Dispersion 27
3.3. Differential ZQC/DQC Decay Rates 30
3.4. ZZ-Exchange 30
3.5. Residual Dipolar Couplings 31
4. Micro- to Millisecond Motions: Solid State NMR 35
4.1. Dynamic Interference: SRI 35
4.2. CODEX and Chemical Exchange 38
4.3. Order Parameters Based on DCs 40
4.4. Relaxation Rate parameters: R1, R2, and R1. 41
4.5. Lineshape Analysis 45
5. Very Slow Motions: 1D MAS Exchange 46
6. Globular Proteins 48
6.1. Comparison of Protein Dynamics Between Solution and Solid 48
6.2. Pico- to Nanosecond motions: Conformational Entropy and Allostery 48
6.3. ms-µs Motions: Biological Function 51
6.3.1. Protein Folding 51
6.3.2. Catalysis and Allosteric Regulation 52
7. Membrane Proteins 54
7.1. Retinal Proteins 54
7.1.1. Bacteriorhodopsin (bR) 54
7.1.2. Sensory Rhodopsin and Proteorhodopsin 58
7.2. Other Proteins 60
8. Conclusion 61
Acknowledgements 62
References 62
Chapter Two: Recent Progress in the Solid-State NMR Studies of Short Peptides: Techniques, Structure and Dynamics 78
1. Introduction 79
2. Development of the New Solid-State NMR Techniques Useful in Structural Studies of Peptides 81
2.1. 1H Solid-State NMR 81
2.2. 13C and 15N Sensitivity under Fast and Medium Magic-Angle Spinning 83
2.3. Two-Dimensional Correlations under F-MAS 89
2.3.1. 1H-13C and 1H-15N HETCOR Correlations 89
2.3.2. 13C-13C and 15N-15N HOMCOR Correlations 91
2.4. Quadrupolar Nuclei 93
3. Molecular Dynamics of Peptides in the Solid State 94
3.1. Probing the Dynamics in Different Time Scales 95
3.2. Tools for Analysis of the Local Molecular Motions of Peptides in the Solid State 98
3.2.1. Relaxation Times 98
3.2.2. Chemical Shift Anisotropy 102
3.2.3. Investigation of the Dynamics by Deuterium Solid-State NMR: Line-Shape Analysis 106
3.2.4. Heteronuclear Dipolar Recoupling Sequences 112
4. Polymorphism and Solvatomorphism of Peptides 116
4.1. Solid-State NMR Study of Polymorphs and Solvatomorphs 117
4.1.1. Ala-Ala-Ala Tripeptide-The Case Study 122
5. Complementarity of Theoretical and NMR Methods in Assignment of the Solid-State Structure of Peptides 126
5.1. Techniques Used for Calculations of NMR Parameters in the Solid State 129
5.2. Theoretical Methods as a Tool for Structure Assignment of Peptides in the Solid State 130
5.3. Fine Refinement of Peptide Crystals with Molecular Disorder 135
5.4. Theoretical Methods Versus Molecular Motion 140
6. Concluding Remarks 142
Acknowledgement 143
References 143
Chapter Three: Solid-State 17O NMR Studies of Biomolecules 156
1. Introduction 157
2. NMR Tensor Parameters 160
3. NMR Methodologies 163
3.1. Site-Specific Spectral Resolution 164
3.1.1. Single-Crystal NMR 164
3.1.2. Magic-Angle Spinning 165
3.1.3. MQMAS and STMAS 166
3.1.4. Dynamic Angle Spinning and Double Rotation 168
3.2. Detection Sensitivity Enhancement 169
3.2.1. Isotopic Enrichment and High Magnetic Field 169
3.2.2. Spin Population Transfer Experiments 170
3.2.3. Dynamic Nuclear Polarization 171
3.2.4. Cryo-MAS 172
3.2.5. Cross-polarization 173
3.3. Correlation NMR Experiments 174
3.4. Quantum Chemical Calculations 178
3.4.1. Molecular Cluster Model 179
3.4.2. Periodic Crystal Lattice 180
3.5. Basic NMR Experimental Considerations 180
3.6. General Schemes for Determining the Tensor Parameters 182
3.6.1. Single Oxygen 183
3.6.2. Multiple Oxygens 183
4. 17O NMR Studies of Biomolecules 186
4.1. Proteins 189
4.1.1. Amino Acids 189
4.1.2. Peptides 191
4.1.3. Proteins 195
4.2. Nucleic Acids 197
4.3. Carbohydrates 198
4.4. Recent Progress on Organic Molecules of Biological Relevance 201
4.4.1. Carboxylic Acids and Carboxylates 201
4.4.2. C-Nitroso Compounds 204
4.4.3. Keto Acids 204
4.4.4. Sulfonic Acids 205
5. Concluding Remarks 206
Acknowledgements 207
Appendix 208
References 224
Chapter Four: Solid-State Nuclear Magnetic Resonance in Pharmaceutical Compounds 232
1. Introduction 233
2. SSNMR Techniques 236
2.1. 1D High-Resolution SSNMR Experiments 236
2.1.1. Diluted Spins 236
2.1.2. High-Resolution 1H NMR MAS 238
2.2. 2D SSNMR Experiments 240
2.3. First Principles Calculations 241
2.4. Relaxation Time Measurements 241
2.5. Multinuclear SSNMR 242
3. SSNMR of Pharmaceutical Compounds 243
3.1. API Characterization 243
3.2. Polymorphism 248
3.3. Pharmaceutical Complexes with Cyclodextrins 257
3.4. Salts and Cocrystals 261
3.5. NMR Crystallography 267
3.6. Tablet Characterization 270
4. Conclusions 271
5. Table of Compounds 271
Acknowledgements 273
References 273
Chapter Five: Covariance NMR and Small Molecule Applications 282
1. Introduction 283
2. On the Theory of Covariance NMR 284
2.1. The General Description 284
2.2. Types of Covariance Transformations in NMR 289
2.2.1. The Classification of Covariance NMR 289
2.2.2. Some Aspects of the Workings of 4D NMR 291
2.2.3. Matrix Regularization in Covariance NMR 292
2.2.4. The Transition from Indirect to Unsymmetrical Indirect Covariance 292
2.2.5. The Workings of Generalized Indirect Covariance NMR 293
2.3. Examples of Covariance Transformations 295
2.4. Artefacts in Covariance NMR Spectra 300
2.5. The Determination of the Non-Linear Signal-to-Noise Ratio 301
2.6. Asynchronous Spectra-The Neglected Imaginary Part 302
2.6.1. General Aspects of Asynchronous Spectra 302
2.6.2. Applications of Asynchronous Spectra 304
2.7. Heterospectroscopy 305
3. Software for Covariance NMR Processing 307
4. Covariance and NUS-The Combination of Two Approaches to Fast Methods 311
5. Applications of Covariance NMR to Small Molecules 317
5.1. Direct Covariance 317
5.1.1. Solution State 317
5.1.2. Solid State 320
5.2. Indirect Covariance 321
5.2.1. Solution State 321
5.2.2. Solid State 327
5.3. Unsymmetrical and Generalized Indirect Covariance 329
5.4. Multidimensional Covariance 344
5.4.1. Triple Rank 344
5.4.2. 4D NMR 345
5.5. Synchronous and Asynchronous Spectra 346
5.6. Statistical Analysis of NMR Spectra in the Field of Metabolomics 347
5.7. Other Covariance Applications in NMR Spectroscopy 349
6. Conclusion 351
Acknowledgements 352
References 352
Index 362
References
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| Erscheint lt. Verlag | 22.7.2014 |
|---|---|
| Sprache | englisch |
| Themenwelt | Naturwissenschaften ► Chemie ► Analytische Chemie |
| Naturwissenschaften ► Physik / Astronomie ► Elektrodynamik | |
| Technik | |
| ISBN-10 | 0-12-800327-8 / 0128003278 |
| ISBN-13 | 978-0-12-800327-5 / 9780128003275 |
| Haben Sie eine Frage zum Produkt? |
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