This study deals with a novel molecular simulation technique, named adiabatic bias molecular dynamics (MD), which provides a simple and reasonably inexpensive route to generate MD trajectories joining points in conformational space separated by activation barriers. Because of the judicious way the biasing potential is updated during the MD runs, the technique allows with some additional effort the computation of the free energy change experienced during the trajectory. The adiabatic bias method has been applied to a nontrivial problem: The unfolding of an atomistic model of lysozyme. Here, the radius of gyration (R-g) was used as a convenient reaction coordinate. For changes in R-g between 19.7 and 28 Angstrom, we observe a net loss of the native tertiary structure of lysozyme. At the same time, secondary structure elements such as alpha-helices are retained although some of the original order is diminished. The calculated free energy profile for the unfolding transition shows a monotonous increase with R-g and depends crucially on the nonbonded cutoff used in the potential model.