Slowing down single-molecule trafficking through a protein nanopore reveals intermediates for peptide translocation.

ABSTRACT: The microscopic details of how peptides translocate one at a time through nanopores are crucial determinants for transport through membrane pores and important in developing nano-technologies. To date, the translocation process has been too fast relative to the resolution of the single molecule techniques that sought to detect its milestones. Using pH-tuned single-molecule electrophysiology and molecular dynamics simulations, we demonstrate how peptide passage through the α-hemolysin protein can be sufficiently slowed down to observe intermediate single-peptide sub-states associated to distinct structural milestones along the pore, and how to control residence time, direction and the sequence of spatio-temporal state-to-state dynamics of a single peptide. Molecular dynamics simulations of

SUBMITTER: Mereuta L 

PROVIDER: S-EPMC3902492 | biostudies-literature | 2014 Jan

REPOSITORIES: biostudies-literature