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NMR protein Spectroscopy
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  • NMR protein Spectroscopy
ID: 174566
John Cavanagh, Wayne J. Fairbrother, Arthur G. Palmer, III, Nicholas J. Skelton, Mark Rance
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Protein NMR Spectroscopy combines a comprehensive theoretical treatment of NMR spectroscopy with macromolecules in solution. Beginning with simple theoretical models and experimental techniques, Protein NMR Spectroscopy develops the ultimate reflexive experiments.

Important new technologies and applications of NMR spectroscopy have been published in 1996. TROSY and deuterium labeling for application large macromolecules, and experimental techniques for characterizing conformational dynamics. In addition, methods of instrumentation and signal acquisition, field gradients, multidimensional spectroscopy, and structure calculation are updated and enhanced.

Protein NMR Spectroscopy is a biochemists, chemists, biophysicists, and structural biologists who utilize NMR spectroscopy.

· 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

Preliminary Table of Contents
1. Classical NMR Spectroscopy
2. Theoretical Description of NMR Spectroscopy
3. Experimental Aspects of NMR Spectroscopy
4. Multi-Dimensional NMR Spectroscopy
5. Relaxation and Dynamic Processes
6. Experimental 1 H NMR Methods
7. Heteronuclear NMR Experiments
8. Experimental NMR Relaxation Methods
9. Larger Proteins and Molecular Interactions
10. Sequential Assignment, Structure Determination and Other Applications
174566

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