The results are a continuation of earlier research at Associate Professor Bjørn Panyella Pedersen's research group at the Department of Molecular Biology and Genetics. A major challenge to make progress in the field is to obtain structures of STPs in different conformations.
PhD Student and first author Laust Bavnhøj explains: "The STPs are highly dynamic membrane proteins that undergoes large conformational changes during transport. This flexibility present a great challenge as conformational stabilization is needed in order to facilitate structure solution by X-ray crystallography. This challenge was exacerbated because we needed the transporter in a very specific conformation in order to answer our questions. Based on our previous work, we could design mutants that worked to destabilize an outward facing conformation. This allowed us to break the "conformational dead water" and push our protein into a new inward facing conformation."