Microtech 2011

A Study of Protein Filaments Sliding through Solid-State Nanopores

A. McMullen, M. Mihovilovic, D. Stein, J.X. Tang
Brown University, US

Keywords: solid-state nanopore, single molecule study, F-actin


The use of nanopores to study DNA has been the topic of intense research over the past decade. Nanopores have been used to probe the structure and electro-physical properties of DNA. These studies have been vitally important for several reasons. The translocation of DNA through nanopores is biologically relevant, as its chemical variant RNA undergoes a similar process when it crosses the cell’s nuclear membrane into the cytoplasm. Also, these studies shed light on many intriguing phenomena of polymer translocation, using DNA as a model charged and semi-flexible polymer. We have expanded the use of nanopores to the study of another extremely important class of biological polymers: protein filaments such as the filamentous actin (F-actin). Actin filaments are essential for many crucial biological functions such as cellular shape change and motility. Whereas DNA is a flexible polymer with a persistence length of 100 nm, F-actin is much stiffer, with a persistence length over 10 μm. This hundred-fold difference presents different constraints on its interaction with a nanopore, providing an interesting deviation from conventional nanopore studies. We present in this report preliminary findings of this new study, including the electric signature, the translocation time and frequency of the protein filaments.

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