In single-molecule experiments forces can be exerted directly on individual molecules and their response can be followed as a function of time. These experiments reveal fundamentally novel and unique information on the structure, dynamics, and interactions of individual biomolecules. In collaboration with Dr. Szabo (NIDDK, NIH), we have continued our development of formalisms to extract accurate kinetic and thermodynamic information from single-molecule force spectroscopy experiments. We could show how system free energies can be transformed into the underlying molecular free energy surface, which is the quantity of interest (1). As part of this work, we also developed a theoretical description of the kinetics of rupture under force in a framework similar to a reaction-diffusion model. 1. G. Hummer, A. Szabo, Free energy profiles from single-molecule pulling experiments, Proc. Natl. Acad. Sci. USA 107, 21441-21446 (2010).