Determination of local movements of the FG-loop and α-helix of sodium-calcium exchanger NCX1.1 upon binding of calcium ions using EPR

Abstract

The structural analysis of the sodium-calcium exchanger NCX1.1 is presented in this thesis. I explore the background information and previous research detailing NCX1.1 and its mechanism. I also explain some of the technical and important details of the primary method used in this research, which is electron paramagnetic resonance (EPR). Using EPR, I found that a small alpha-helix of NCX1.1 undergoes no conformational change upon the binding of calcium ions to the protein. Also, the results suggest that another region, a small unstructured loop, may undergo some change when calcium ions are bound. This opens the door to future research on this protein and the mechanism of its activity.