We are studying the structural and dynamic properties of integral membrane proteins and peptides. These projects are funded by the NIH and NSF.
Solid-State NMR Spectroscopy is a very valuable tool for probing the structure of membrane proteins. The 13C solid-state NMR spectrum on the right indicates that the transmembrane domain (Leu-39) of PLB is a-helical (3C peak at 177 ppm; shown in (A)). The cytoplasmic domain (Ala-15) reveals two unique 13C resonance consisting of 2 different a-helical structural conformations.
We are developing new approaches to study the structural topology of membrane proteins using EPR spectroscopy. The alignment of a spin-labeled protein inside a membrane with respect to the magnetic field reveals an EPR spectrum that is orientational dependent. The corresponding EPR spectra will indicate the helical tilt of the protein with respect to the membrane. This project is funded by the NSF.
The Lorigan research group is studying the structural and dynamic properties of integral membrane proteins using state-of-the-art magnetic resonance techniques. These projects are funded by the NIH and NSF.