This collection of readily reproducible methods using the latest advances in NMR technology includes methods for high-level recombinant protein expression using sophisticated isotopic labeling strategies, TROSY methods for the study of structure and dynamics, and methods for the acquisition and interpretation of residual dipolar coupling data. There are also applications of dynamics measurements on multiple timescales, new developments in NMR data analysis, structure calculation protocols, and solid-state methods. The protocols follow the successful Methods in Molecular Biology series format, each offering detailed laboratory instructions, an introduction outlining the principle behind the technique, lists of equipment and reagents, and tips on troubleshooting and avoiding known pitfalls.Carrying on in the tradition of its much praised earlier edition, A. Kristina Downing has selected new protocols describing the many recent advances in NMR methodology that are revolutionizing the field. Described in step-by-step detail by established hands-on experts, these readily reproducible techniques include methods for high-level recombinant protein expression using sophisticated isotopic labeling strategies, TROSY methods for the study of structure and dynamics, and methods for the acquisition and interpretation of residual dipolar coupling data. There are also applications of dynamics measurements on multiple timescales, new developments in NMR data analysis, structure calculation protocols, and a comprehensive chapter on solid-state methods for the study of membrane proteins. The protocols follow the successful Methods in Molecular Biology series format, each offering detailed laboratory instructions, an introduction outlining the principle behind the technique, lists of equipment and reagents, and tips on troubleshooting and avoiding known pitfalls.§State-of-the-art and highly practical, Protein NMR Techniques, 2nd Ed., makes accessible to all NMR laboratories proven techniques that are powerfully transforming the speed, accuracy, and size limit of our ability to characterize biological macromolecules.
