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SINGLE MOLECULE MECHANICS: EXPLORING THE COMPLEX PROTEIN UNFOLDING LANDSCAPE Alastair Smith Department of Physics and Astronomy and Astbury Centre for Structural Molecular Biology, University of Leeds, UK The effect of applied force on the energy landscape that describes protein conformation is an exciting and challenging topic in molecular biophysics. Recently it has become possible to use nanotechnology tools such as the atomic force microscope and laser tweezers to manipulate individual molecules and explore the complex free energy landscape that describes protein conformation. The method of mechanically unfolding single proteins using the atomic force microscope has been applied to a handful of naturally occurring and synthetic hetero- and homo-polyproteins. However, until now it has only been possible to unfold a protein by pulling on the two ends of the molecule, and this only allows a single pathway through the energy landscape to be explored. Here, experimental data and molecular dynamics simulations of the unfolding of a single protein due to force applied in two different directions will be presented and discussed. These measurements open the way for a detailed exploration of the energy landscape and a thorough comparison between experiment and theory.