Situated in the new Schweitzer Hall Addition, Department of Biochemistry at the University of Missouri - Columbia, the Tang laboratory utilizes state-of-the-art nuclear magnetic resonance or NMR and various biochemical/biophysical/computational techniques to characterize macromolecular structure and dynamics in solution.
Over the last half a century, structure determination of macromolecules at atomic-resolution has been mostly focused on obtaining a single conformation that agrees with the experimental data. With an increasing appreciation of the vital coupling between conformational fluctuation of a macromolecule (i.e. dynamics) and its function (e.g., folding, allostery and macromolecular association), a new paradigm of structure determination is emerging in recent years that aims at obtaining a structure ensemble sampled by the subject protein.
The Tang laboratory applies novel paramagnetic NMR method including paramagnetic relaxation enhancement (PRE), pseudo-contact shift (PCS) and residual dipolar coupling (RDC), to characterize ensemble conformations of macromolecules. Owing to the large magnetic moment of an unpaired electron, the paramagnetic effects provide a sensitive measurement of the lowly populated excited states. Combined with other low-resolution, localized approaches such as small angle scattering and fluorescence energy transfer, the macromolecular dynamics is being directly visualized in the Tang laboratory.