Mechanical unfold and transport of Green Florescent Protein through a nanopore

We report the unfold and trans-location of Green Fluorescent protein (GFP) mechanically by a constant force acting parallel along the axis of nanopore. A coarse-grained numerical model (Go-model) were implemented both for the protein and the nanopore. Detail description of each peptide unfold by the constant force is presented. Depending on the GFP topological structure, {beta}-sheet barrel, the protein unfold and transport as a double loop conformation in the confinement geometry. The result is compared with maltose binding protein (MBP), having majority of alpha helix, which unfold and trans-locate as single profile conformation through nanopore. The result emphasis that protein with different topological structure unfold and trans-locate in different fashion depending on their native fold structure.