Use of Relaxation Enhancements in a Paramagnetic Environment for the Structure Determination of Proteins Using NMR Spectroscopy

摘要

NMR spectroscopy has developed into one of the principal methods in structural biology and enables not only the determination of the three-dimensional structure but also of the dvnamic aspects of biological macromolecules. Methodological developments in the last decade (e.g. transverse dipolar-optimized spectroscopy (TROSY), residual dipolar couplings (RDCs), deuteration, stereoarray isotope labeling (SAIL), methyl-TROSY, and direct ~(13)C detection) have expanded the size of proteins that can be analyzed by solution-state NMR spectroscopy.