The Evolution of 3D NMR Isotope Labeling Techniques in Determining the 3D Structure of Large Proteins

The size of macromolecular structures that can be solved by nuclear magnetic resonance (NMR) spectroscopy has dramatically increased over the years in the evolution of stable isotope labeling methods. Studies in uniform 13C/15N labeling, random fractional deuterium labeling, selectively labeling amino acids and stereo-array isotope labeling (SAIL) are provided as examples of this evolution of protein NMR spectroscopy as the methods expand to larger proteins by overcoming spectroscopic and structural challenges