Protein NMR Spectroscopy - Principles and Practice

Protein NMR Spectroscopy provides a complete introduction to solution NMR spectroscopy for determining three-dimensional structures, dynamical properties, and intermolecular interactions of proteins. The Second Edition of this now classic text provides an authoritative presentation of the theoretical principles and experimental practices required for the mort sophisticated applications of solution NMR spectroscopy to explicate the molecular basis of protein function, which in turn is increasingly important for understanding mechanisms of disease and for developing novel therapeutic approaches. Incorporating new chapters on spin relaxation methods and on methods for studying larger macromolecules and molecular interactions, the thoroughly revised Second Edition also offers new coverage of important topics that include residual dipolar couplings, transverse relaxation optimized spectroscopy, and deuterium NMR spectroscopy.
In addition, the treatments of instrumentation and signal acquisition, radiofrequency pulse techniques, pulsed field gradients, spin relaxation, and triple resonance spectroscopy have been extensively updated and enhanced. Key features of Protein NMR Spectroscopy include: Theoretical principles important for biological NMR spectroscopy; Implementation and optimization of modern multi-dimensional NMR experiments; Experimental protocols for investigations of protein structures, interactions, and dynamics; Comprehensive example NMR spectra for ubiquitin and calbindin D28k.
Protein NMR Spectroscopy will be of interest to advanced undergraduate and graduate students as well as practicing biochemists, chemists, biophysicists, and structural biologists who utilize NMR spectroscopy as a research tool or wish to remain abreast of the latest developments in this increasingly important area.