Protein NMR techniques 3rd Edition by Alexander Shekhtman, David S Burz ISBN 1617794805 9781617794803
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ISBN 10: 1617794805
ISBN 13: 9781617794803
Author: Alexander Shekhtman, David S Burz
The field of protein NMR spectroscopy has rapidly expanded into new areas of biochemistry, molecular biology and cell biology research that were impossible to study as recently as ten years ago. This third edition of Protein NMR Techniques, expands upon the previous editions with current, detailed authoritative but down-to-earth descriptions of new methodologies. These include techniques for NMR sample preparation, solution and solid state NMR methodologies and data processing. Written in the highly successful Methods in Molecular Biology™ series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and key tips on troubleshooting and avoiding known pitfalls.
Protein NMR techniques 3rd Table of contents:
Chapter 1: Introduction to Protein NMR
1.1 Overview of NMR Spectroscopy
1.2 Historical Development of Protein NMR
1.3 Advantages and Limitations of Protein NMR
1.4 Comparison with Other Structural Biology Techniques
1.5 Applications in Biochemistry and Drug Discovery
Chapter 2: Principles of NMR Spectroscopy
2.1 Nuclear Spin and Magnetic Properties
2.2 Chemical Shift and Shielding
2.3 Spin-Spin Coupling
2.4 Relaxation Mechanisms (T1, T2)
2.5 Sensitivity and Resolution in Protein NMR
Chapter 3: Sample Preparation for Protein NMR
3.1 Isotopic Labeling Strategies (^15N, ^13C, ^2H)
3.2 Protein Expression and Purification
3.3 Buffer Selection and Sample Conditions
3.4 Protein Solubility and Stability Considerations
3.5 Concentration and Volume Optimization
Chapter 4: One-Dimensional (1D) NMR Techniques
4.1 ^1H NMR Spectroscopy
4.2 ^13C and ^15N NMR Basics
4.3 1D Experiments for Protein Folding and Stability
4.4 Limitations and Interpretation of 1D Data
Chapter 5: Two-Dimensional (2D) NMR Techniques
5.1 COSY, TOCSY, and NOESY
5.2 HSQC and HMQC for Heteronuclei
5.3 Sequential Assignment Strategies
5.4 Structure Determination Using 2D NMR
Chapter 6: Three- and Four-Dimensional NMR Techniques
6.1 3D Triple-Resonance Experiments
6.2 4D NMR for Large Proteins
6.3 Resolving Overlapping Signals
6.4 Advanced Assignment Strategies
Chapter 7: Dynamics and Relaxation Studies
7.1 Relaxation Measurements (T1, T2, NOE)
7.2 Internal Motions and Protein Flexibility
7.3 Conformational Exchange and Kinetics
7.4 Applications in Ligand Binding Studies
Chapter 8: Protein-Ligand and Protein-Protein Interactions
8.1 Mapping Binding Sites
8.2 Chemical Shift Perturbation Analysis
8.3 Saturation Transfer Difference (STD) NMR
8.4 Paramagnetic NMR and PRE Techniques
Chapter 9: Solid-State NMR for Proteins
9.1 Principles of Solid-State NMR
9.2 Magic Angle Spinning (MAS)
9.3 Applications in Membrane Proteins
9.4 Structural Studies of Amyloids and Aggregates
Chapter 10: Computational Approaches and NMR Data Analysis
10.1 NMR Data Processing Software
10.2 Structure Calculation and Validation
10.3 Molecular Dynamics Integration
10.4 Automated Assignment Methods
Chapter 11: Case Studies and Applications
11.1 Enzyme Structure and Dynamics
11.2 Protein Folding Studies
11.3 Drug Discovery and Design
11.4 NMR in Structural Genomics
Chapter 12: Future Directions and Emerging Techniques
12.1 Hyperpolarization Methods
12.2 Cryogenic NMR and Sensitivity Enhancements
12.3 NMR in Large Protein Complexes
12.4 Integration with Other Structural Techniques
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