Dynamicforce spectroscopy provides unique opportunities for probing the freeenergy landscape of biomolecules. However, even if it providesinformation on the chain extension, it cannot supply full details ofthe populated structures. This is especially true in the case ofmulti-domain proteins for which the complexity of the fold translatesinto many unfolding scenarios. I will present our investigations intothe role of protein-protein interactions  during biomechanicalunfolding reactions of multi-domain protein complexes coveringvarious cellular functions from fusion to cytoskeletal support inexperimental time . To obtain the force extension curves usingexperimental pulling speeds, we employed a coarse-grained minimalistmodel (SOP) of proteins. I will discuss the signature of theprotein-protein interactions as a function of the applied vectorforce, and the connection between the shape of the force peaks andthe degree of cooperativity in the protein complex.

Large-scale
molecular simulations of dynamics in mechanical proteins

242nd National Meeting (2011)

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Large-scale molecular simulations of dynamics in mechanical proteins