Protein NMR Spectroscopy: Principles and Practice
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Table of contents
- Protein NMR Spectroscopyiii
- Copyright Pageiv
- Prefacev
- Preface to the First editionvii
- Acknowledgementsxi
- Table of Contentsxiii
- CHAPTER 1. CLASSICAL NMR SPECTROSCOPY1
- 1.1 NuclearMagnetism2
- 1.2 The Bloch Equations7
- 1.3 The One-Pulse NMR Experiment16
- 1.4 Linewidth18
- 1.5 Chemical Shift21
- 1.6 Scalar Coupling and Limitations of the Bloch Equations23
- References27
- CHAPTER 2. THEORETICAL DESCRIPTION OF NMR SPECTROSCOPY29
- 2.1 Postulates of Quantum Mechanics29
- 2.2 The DensityMatrix37
- 2.3 Pulses and Rotation Operators50
- 2.4 Quantum Mechanical NMR Spectroscopy54
- 2.5 Quantum Mechanics of Multispin Systems58
- 2.6 Coherence70
- 2.7 Product Operator Formalism77
- 2.8 Averaging of the Spin Hamiltonians and Residual Interactions102
- References112
- CHAPTER 3. EXPERIMENTAL ASPECTS OF NMR SPECTROSCOPY114
- 3.1 NMR Instrumentation114
- 3.2 Data Acquisition124
- 3.3 Data Processing136
- 3.4 PulseTechniques165
- 3.5 Spin Decoupling201
- 3.6 B0 Field Gradients217
- 3.7 Water SuppressionTechniques221
- 3.8 One-Dimensional1H NMR Spectroscopy234
- References267
- CHAPTER 4. MULTIDIMENSIONAL NMR SPECTROSCOPY271
- 4.1 Two-Dimensional NMR Spectroscopy273
- 4.2 CoherenceTransfer andMixing280
- 4.3 Coherence Selection, Phase Cycling, and Field Gradients292
- 4.4 Resolution and Sensitivity326
- 4.5 Three- and Four-Dimensional NMR Spectroscopy327
- References331
- CHAPTER 5. RELAXATION AND DYNAMIC PROCESSES333
- 5.1 Introduction and Survey of Theoretical Approaches334
- 5.2 TheMaster Equation351
- 5.3 SpectralDensity Functions365
- 5.4 RelaxationMechanisms370
- 5.5 Nuclear Overhauser Effect388
- 5.6 Chemical Exchange Effects in NMR Spectroscopy391
- References402
- CHAPTER 6. EXPERIMENTAL 1H NMRMETHODS405
- 6.1 Assessment of the1D1H Spectrum406
- 6.2 COSY-Type Experiments409
- 6.3 Multiple-Quantum Filtered COSY437
- 6.4 Multiple-Quantum Spectroscopy463
- 6.5 TOCSY486
- 6.6 Cross-Relaxation NMR Experiments502
- 6.7 1H 3DExperiments525
- References529
- CHAPTER 7. HETERONUCLEAR NMR EXPERIMENTS533
- 7.1 Heteronuclear Correlation NMR Spectroscopy535
- 7.2 Heteronuclear-Edited NMR Spectroscopy581
- 7.3 13C-13C Correlations:The HCCH-COSYand HCCH-TOCSY Experiments601
- 7.4 3DTriple-Resonance Experiments613
- 7.5 Measurement of Scalar Coupling Constants656
- 7.6 Measurement of Residual Dipolar Coupling Constants665
- References673
- CHAPTER 8. EXPERIMENTAL NMR RELAXATION METHODS679
- 8.1 Pulse Sequences and ExperimentalMethods680
- 8.2 Picosecond-Nanosecond Dynamics685
- 8.3 Microsecond-Second Dynamics702
- References721
- CHAPTER 9. LARGER PROTEINS AND MOLECULAR INTERACTIONS725
- 9.1 Larger Proteins725
- 9.2 Intermolecular Interactions753
- 9.3 Methods for Rapid Data Acquisition769
- References775
- CHAPTER 10. SEQUENTIAL ASSIGNMENT, STRUCTURE DETERMINATION, AND OTHER APPLICATIONS781
- 10.1 ResonanceAssignment Strategies782
- 10.2 Three-Dimensional Solution Structures796
- 10.3 Conclusion813
- References814
- TABLE OF SYMBOLS819
- LIST OF FIGURES825
- LIST OF TABLES837
- SUGGESTED READING839
- INDEX841
- SPIN-1/2 PRODUCT OPERATOR EQUATIONS887
- TABLE OF CONSTANTS888
Protein NMR Spectroscopy combines a comprehensive theoretical treatment of NMR spectroscopy with an extensive exposition of the experimental techniques applicable to proteins and other biological macromolecules in solution. Beginning with simple theoretical models and experimental techniques, Protein NMR Spectroscopy develops the complete repertoire of theoretical principles and experimental techniques necessary for understanding and implementing the most sophisticated NMR experiments.
Important new techniques and applications of NMR spectroscopy have emerged since the first edition of this extremely successful book was published in 1996. The second edition includes new sections describing measurement and use of residual dipolar coupling constants for structure determination, TROSY and deuterium labeling for application to large macromolecules, and experimental techniques for characterizing conformational dynamics. In addition, the treatments of instrumentation and signal acquisition, field gradients, multidimensional spectroscopy, and structure calculation are updated and enhanced.
Protein NMR Spectroscopy is written as a graduate-level textbook and will be of interest to biochemists, chemists, biophysicists, and structural biologists who utilize NMR spectroscopy or who wish to understand the latest developments in this field.
· Provides an understanding of the theoretical principles important for biological NMR spectroscopy
· Demonstrates how to implement, optimize and troubleshoot modern multi-dimensional NMR experiments
· Allows for the capability of designing effective experimental protocols for investigations of protein structures and dynamics
· Includes a comprehensive set of example NMR spectra of ubiquitin provides a reference for validation of experimental methods
Important new techniques and applications of NMR spectroscopy have emerged since the first edition of this extremely successful book was published in 1996. The second edition includes new sections describing measurement and use of residual dipolar coupling constants for structure determination, TROSY and deuterium labeling for application to large macromolecules, and experimental techniques for characterizing conformational dynamics. In addition, the treatments of instrumentation and signal acquisition, field gradients, multidimensional spectroscopy, and structure calculation are updated and enhanced.
Protein NMR Spectroscopy is written as a graduate-level textbook and will be of interest to biochemists, chemists, biophysicists, and structural biologists who utilize NMR spectroscopy or who wish to understand the latest developments in this field.
· Provides an understanding of the theoretical principles important for biological NMR spectroscopy
· Demonstrates how to implement, optimize and troubleshoot modern multi-dimensional NMR experiments
· Allows for the capability of designing effective experimental protocols for investigations of protein structures and dynamics
· Includes a comprehensive set of example NMR spectra of ubiquitin provides a reference for validation of experimental methods