Abstract
One of the ultimate goals of structural biology is to understand how proteins exerttheir functions at atomic resolution in order to modulate their activities for applicationssuch as drug discovery. Nuclear Magnetic Resonance (NMR) spectroscopy isincreasingly becoming an important method for characterizing the three-dimensionalstructure of proteins under near physiological conditions. NMR is not only a powerfulmethod for elucidating the three-dimensional structures of proteins in aqueous solution,but also a convenient method for studying protein-ligand interactions as well as proteindynamics. NMR studies, however, require the assignment of individual signals toindividual NMR-active atoms in proteins. This so-called resonance assignment ofproteins can be a time-consuming and laborious process. In addition, the number ofNMR signals increases proportionally to the molecular size of the proteins. Therefore,NMR studies of larger proteins are increasingly time-consuming and challenging.The use of stable isotopes such as
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