The North Jersey ACS NMR Topical Group proudly presents its February meeting at the Fuji Japanese Sushi & Seafood on Wednesday, February 20, 2013.
Dr. Nate Traaseth
Assistant Professor, Department of Chemistry, New York University
“Structural Studies of Small Multidrug Resistance Membrane Proteins by Oriented and Magic-Angle-Spinning Solid-State NMR Spectroscopy in Lipid Bilayers”
Register online here or via e-mail to Swapna Gurla at firstname.lastname@example.org.
Fuji Japanese Sushi & Seafood
1345 US Rt 1, North Brunswick, NJ 08902
Please note that Pathmark is no more.
Fuji is on US 1 Southbound.
[ Directions ]
6:00 pm Dinner
7:00 pm Seminar
Dinner cost: $15 ($5 for student, postdoc or retired). No charge for seminar only.
Multidrug resistance (MDR) is a pervasive clinical problem that reduces the effectiveness of treatment against bacterial infections, viral infections, and cancer. Efflux of drugs across the lipid bilayer by MDR membrane protein transporters is one way in which resistance is conferred to the host organism or cell. To derive a structure/function relationship for this class of proteins, our study uses the small multidrug resistance (SMR) family as a model system for deciphering the mechanism of transport with the long-term goal of decoding the evolutionary importance of the transporter family. We used solid-state NMR (SSNMR) spectroscopy to study the topology and structure of EmrE in liposomes (magic-angle-spinning or MAS) and magnetically aligned lipid bilayers (oriented SSNMR or O-SSNMR). The MAS experiments were used to map chemical shift perturbations upon drug binding while the O-SSNMR experiments revealed the change in helix orientation upon binding and transport. Together these complementary techniques showed that drug binding perturbs both the structure of EmrE as well as the helical orientations with respect to the lipid bilayer.