1: Classical NMR Spectroscopy 2: Theoretical Description of NMR Spectroscopy 3: Experimental Aspects of NMR Spectroscopy 4: Multidimensional NMR Spectroscopy 5: Relaxation and Dynamic Processes 6: Experimental 1h 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
Protein NMR Spectroscopy, Second Edition combines a comprehensive theoretical treatment of NMR spectroscopy with an extensive exposition of the experimental techniques applicable to proteins and other biological macromolecules in solution.
Beginning with simple theoretical models and experimental techniques, the book develops the complete repertoire of theoretical principles and experimental techniques necessary for understanding and implementing the most sophisticated NMR experiments.
Important new techniques and applications of NMR spectroscopy have emerged since the first edition of this extremely successful book was published in 1996. This updated version includes new sections describing measurement and use of residual dipolar coupling constants for structure determination, TROSY and deuterium labeling for application to large macromolecules, and experimental techniques for characterizing conformational dynamics. In addition, the treatments of instrumentation and signal acquisition, field gradients, multidimensional spectroscopy, and structure calculation are updated and enhanced.
The book is written as a graduate-level textbook and will be of interest to biochemists, chemists, biophysicists, and structural biologists who utilize NMR spectroscopy or wish to understand the latest developments in this field.