Elsevier S & T

Nuclear Magnetic Resonance of Biological Macromolecules, Part C: Methods in Enzymology

James, Thomas L.

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Table of contents
  • Copyright Pageiv
  • Table of Contentsv
  • Contributors to Volume 394ix
  • Volumes in Seriesxv
  • Section I: Techniques: Spectral, Experimental, and Analytical1
  • Chapter 1. Identification and Optimization of Protein Domains for NMR Studies3
  • Chapter 2. In-Cell NMR Spectroscopy17
  • Chapter 3. Molecular Fragment Replacement Approach to Protein Structure Determination by Chemical Sh42
  • Chapter 4. Rapid NMR Data Collection78
  • Section II: Proteomics109
  • Chapter 5. An Integrated Platform for Automated Analysis of Protein NMR Structures111
  • Chapter 6. Rapid Assessment of Protein Structural Stability and Fold Validation via NMR142
  • Chapter 7. Determination of Protein Backbone Structures from Residual Dipolar Couplings175
  • Chapter 8. Robotic Cloning and Protein Production Platform of the Northeast Structural Genomics Cons210
  • Chapter 9. Protein Structure Estimation from Minimal Restraints Using Rosetta244
  • Chapter 10. Protein Structure Elucidation from Minimal NMR Data: The CLOUDS Approach261
  • Section III: Challenging Systems for NMR297
  • Chapter 11. Elucidation of the Protein Folding Landscape by NMR299
  • Chapter 12. Membrane Protein Preparation for TROSY NMR Screening321
  • Chapter 13. Solution Structure and Dynamics of Integral Membrane Proteins by NMR: A Case Study Invol335
  • Chapter 14. NMR Experiments on Aligned Samples of Membrane Proteins350
  • Chapter 15. NMR Techniques Used with Very Large Biological Macromolecules in Solution382
  • Chapter 16. Structure Determination of Large Biological RNAs399
  • Section IV: Macromolecular Dynamics417
  • Chapter 17. Hydrodynamic Models and Computational Methods for NMR Relaxation419
  • Chapter 18. Solution NMR Spin Relaxation Methods for Characterizing Chemical Exchange in High-Molecu430
  • Chapter 19. Isotropic Reorientational Eigenmode Dynamics Complements NMR Relaxation Measurements for465
  • Section V: Macromolecular Complexes481
  • Chapter 20. NMR Techniques for Identifying the Interface of a Larger Protein–Protein Complex: Cros483
  • Chapter 21. Enzyme Dynamics During Catalysis Measured by NMR Spectroscopy507
  • Chapter 22. Structure Determination of Protein/RNA Complexes by NMR525
  • Section VI: Ligand Discovery547
  • Chapter 23. Utilization of NMR-Derived Fragment Leads in Drug Design549
  • Chapter 24. Discovery of Ligands by a Combination of Computational and NMR-Based Screening: RNA as a571
  • Author Index589
  • Subject Index621
Book details
  • Vendor Elsevier S & T
  • SKU 9780121827991
  • ISBN-13 9780080549477
  • Author James, Thomas L.
  • Category Science
  • Subject Research & Methodology

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The critically acclaimed laboratory standard, Methods in Enzymology, is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. The series contains much material still relevant today - truly an essential publication for researchers in all fields of life sciences.

Nuclear Magnetic Resonance of Biological Macromolecules, Part C is written with a "hands-on" perspective. That is, practical applications with critical evaluations of methodologies and experimental considerations needed to design, execute, and interpret NMR experiments pertinent to biological molecules.

* One of the most highly respected publications in the field of biochemistry since 1955
* Frequently consulted, and praised by researchers and reviewers alike
* Truly an essential publication for anyone in any field of the life sciences