Dynamics and Energy Contributions for Transport of Unfolded Pertactin through a Protein Nanopore.

ABSTRACT: To evaluate the physical parameters governing translocation of an unfolded protein across a lipid bilayer, we studied protein transport through aerolysin, a passive protein channel, at the single-molecule level. The protein model used was the passenger domain of pertactin, an autotransporter virulence protein. Transport of pertactin through the aerolysin nanopore was detected as transient partial current blockades as the unfolded protein partially occluded the aerolysin channel. We compared the dynamics of entry and transport for unfolded pertactin and a covalent end-to-end dimer of the same protein. For both the monomer and the dimer, the event frequency of current blockades increased exponentially with the applied voltage, while the duration of each event decreased exponentially as a fun

SUBMITTER: Cressiot B 

PROVIDER: S-EPMC4835817 | biostudies-literature | 2015 Sep

REPOSITORIES: biostudies-literature