FBS Colloquia No.349Laboratory for Ultra-High Magnetic Field NMR Spectroscopy

Unveiling protein structure and dynamics with relaxation optimized SAIL NMR

During the past few years, we have been developing the stereo specific isotope labeling method to elucidate the precise structures and dynamics of large molecular weight proteins and protein complexes, which are essential for understanding their biological functions. Using our new isotope-aided NMR method, we successfully observed the extremely narrow aromatic / aliphatic 13C-1H signals for the 80-500 kDa proteins. We have successfully analyzed the structural dynamics of the bacterial flagellar motor protein (FliG) and the PI3K protein, which controls T cell activation signals, utilizing our novel NMR measurement techniques. In this colloquium, we will also discuss the underlying mechanisms of their biological functions.