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Single molecule force spectroscopy provide details of the underlying energysurfaces of proteins which are essential to the understanding of theirunfolding process. Recently, it has been observed experimentally that bypulling proteins in different directions relative to their secondary structure,one can gain a better understanding of the shape of the energy landscape. Weconsider simple lattice models which are anisotropic in nature to study theresponse of a force in unfolding of a polymer. Our analytical solution of themodel, supported by extensive numerical calculations, reveal that the forcetemperature diagrams are very different depending on the direction of theapplied force. We find that either unzipping or shearing kind transitionsdominate the dynamics of the unfolding process depending solely on thedirection of the applied force.

Role of pulling direction in understanding the energy landscape of proteins