A Study of Protein Filaments Sliding through Solid-State Nanopores

摘要

Solid-state nanopores have been used extensively over the past decade as powerful tools to study the structure and dynamics of single molecules of DNA. The use of nanopores has mostly been confined to the study of DNA due to the hope that they may eventually be used to cheaply sequence DNA. We have begun extending nanopores to the study of protein filaments, specifically filamentous actin (F-actin), one of three major components of the cytoskeleton. F-actin is a linear, negatively charged, helical polymer well suited for use in a nanopore setup. F-actin, however, behaves qualitatively different in solution than DNA as a result of their differences in persistence length. This enforces a different set of constraints on an F-actin molecule's interaction with a nanopore, allowing for new insights into the polymer dynamics of translocation through a nanometer-sized pore.