Unknown

Dataset Information

0

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 ?-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 peptide translocation reveal the time- dependent ordering of intermediate structures of the translocating peptide inside the pore at atomic resolution. Calculations of the expected current ratios of the different pore-blocking microstates and their time sequencing are in accord with the recorded current traces.

SUBMITTER: Mereuta L 

PROVIDER: S-EPMC3902492 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature

altmetric image

Publications

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

Mereuta Loredana L   Roy Mahua M   Asandei Alina A   Lee Jong Kook JK   Park Yoonkyung Y   Andricioaei Ioan I   Luchian Tudor T  

Scientific reports 20140127


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  ...[more]

Similar Datasets

| S-EPMC3349906 | biostudies-literature
| S-EPMC3875158 | biostudies-literature
| S-EPMC1965533 | biostudies-literature
| S-EPMC5483527 | biostudies-literature
| S-EPMC7794543 | biostudies-literature
| S-EPMC1599963 | biostudies-literature
| S-EPMC3170403 | biostudies-literature
| S-EPMC9898208 | biostudies-literature
| S-EPMC3664219 | biostudies-literature
| S-EPMC7817135 | biostudies-literature