The atomic resolution insight provided by solid-state NMR is vital for expanding our understanding of membrane biology. Advances in protein structure determination using solid-state NMR data, coupled with proton detection using very fast magic-angle spinning rates in the solid state, have the lab extremely well positioned to tackle these problems. We do this with a combination of the highest quality NMR data and cutting-edge computational methods to determine the structure and dynamics of proteins and membranes.
We seek to study membrane proteins in their native lipids, and determine the effects the lipids bilayer itself has on the protein and understand why they occur via the direct investigation of membranes by solid-state NMR. To do this, we continue to develop techniques for directly probing the structure and dynamics of lipid bilayers by solid-state NMR as well as the effects that different lipid species and small molecules can have on them. At Rutgers we have improved the 31P spectroscopy used to directly observe lipid head-groups. We use very-fast MAS and proton detection to observe lipid-lipid and lipid-protein interactions. We are developing pulse sequences and data analysis workflows to measure precise lipid-protein distances using 1H, 13C, 15N and 31P.