Protein NMR Spectroscopy: Principles and Practice, Third Edition develops the complete repertoire of theoretical principles and experimental techniques necessary for understanding and implementing the most sophisticated NMR experiments applicable to proteins and other biological macromolecules in solution. Important new techniques and applications of NMR spectroscopy have emerged since the second edition of this extremely successful book was published in 2006. This third edition includes new sections describing metalloproteins and the application of paramagnetic effects to protein structural elucidation. In addition, the treatments of residual dipolar coupling, intermolecular protein-ligand interactions, relaxation dispersion techniques and larger proteins and requisite labelling schemes are updated and enhanced. The book is written at a level appropriate for graduate students and practicing biochemists, chemists, biophysicists and structural biologists who utilize NMR spectroscopy as a research tool or who wish to understand the latest developments in the field.
1. Classical NMR Spectroscopy2. Theoretical Description of NMR Spectroscopy3. Experimental Aspects of NMR Spectroscopy4. Multi-Dimensional NMR Spectroscopy5. Relaxation and Dynamic Processes6. Experimental 1H NMR Methods7. Heteronuclear NMR Experiments8. Experimental NMR Relaxation Methods9. Larger Proteins and Molecular Interactions10. Sequential Assignment, Structure Determination and Other Applications