Force-Distance Curves Analysis in Single-Molecule Force Spectroscopy

Single-Molecule Force Spectroscopy is an application of Atomic Force Microscopy, and is used to mechanically unfold proteins, producing Force-Distance (FD) curves. These FD curves can then be analyzed and fitted to identify unfolding pathways and intermediate states. In this thesis we analyze a set of a hundred FD curves of the LmrP integral membrane protein. The main factor complicating this analysis is that, for experimental reasons, there is a different and unknown offset on the distance of each FD curve. We start out by fitting each FD curve with a Worm-Like Chain model, then cluster and align them to identify a main unfolding pathway and two tentative intermediate states.