Nuclear Magnetic Resonance of Biological Macromolecules, Part C: Volume 394

Nuclear Magnetic Resonance of Biological Macromolecules, Part C: Volume 394

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Description

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.
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Product details

  • Hardback | 672 pages
  • 160 x 231.1 x 30.5mm | 1,043.27g
  • Academic Press Inc
  • San Diego, United States
  • English
  • Approx. 150 illustrations; Illustrations, unspecified
  • 0121827992
  • 9780121827991

Table of contents

Identification and optimization of protein domains for NMR studies
In-cell NMR spectroscopy
Molecular Fragment Replacement Approach to Protein Structure Determination by Chemical Shift and Dipolar Homology Database Mining
Cross-correlated relaxation for structure and dynamics
Rapid NMR Data Collection
An Integrated Platform for Automated Analysis of Protein NMR Structures
Rapid Assessment of Protein Structural Stability and Fold Validation via NMR
Determination of Protein Backbone Structures from Residual Dipolar Couplings
Robotic Cloning and Protein Production Platform of the Northeast Structural Genomics Consortium
Protein Structure Estimation From Minimal Restraints Using Rosetta
Protein Structure Elucidation From Minimal Data: The CLOUDS and ABACUS Approaches
Elucidation of the Protein Folding Landscape by NMR
Membrane Protein Preparation for TROSY NMR Screening
Solution structure and dynamics of integral membrane proteins by NMR: a case study involving the enzyme PagP
NMR Experiments on Aligned Samplet of Membrane Proteins
NMR techniques used with very large biological macromolecules in solution
Structure determination of large biological RNAs
Hydrodynamic Models and Computational Methods for NMR relaxation
Solution NMR Spin Relaxation Methods for Characterizing Chemical Exchange in High Molecular Weight Systems
Isotropic Reorientational Eigenmode Dynamics Complements NMR Relaxation Measurements for RNA
NMR techniques for identifying the interface of a larger protein-protein complex: cross and transferred cross-saturation experiments
Enzyme Dynamics During Catalysis Measured by NMR Spectroscopy
Structure determination of protein/RNA complexes by NMR
Utilization of NMR-derived fragment leads in drug design
Discovery of Ligands by a Combination of Computational and NMR-based Screening: RNA as an Example Target
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