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Nuclear magnetic resonance of biological macromolecules. Part C

Author: Thomas L James
Publisher: San Diego, CA : Academic Press, ©2005.
Series: Methods in enzymology, v. 394.
Edition/Format:   Print book : EnglishView all editions and formats
Summary:

Part of the "Methods in Enzymology" series, this work is written with a "hands-on" perspective. It includes practical applications with critical evaluations of methodologies and experimental  Read more...

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Document Type: Book
All Authors / Contributors: Thomas L James
ISBN: 0121827992 9780121827991
OCLC Number: 59100279
Description: xxxvii, 631 pages, [17 leaves of plates] : illustrations (some color) ; 24 cm.
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.
Series Title: Methods in enzymology, v. 394.
Responsibility: edited by Thomas L. James.

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