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. Provides an understanding of the theoretical principles important for biological 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 that provides a reference for validation of experimental methods Features detailed derivations of the density matrix formalism and relaxation theory.