Ultra-fast single-file transport of a simple liquid beyond the collective behavior zone

2016 ◽  
Vol 18 (30) ◽  
pp. 20251-20255 ◽  
Author(s):  
Jiaye Su ◽  
Keda Yang ◽  
Decai Huang
Keyword(s):  
Collective Behavior ◽  
Simple Liquid ◽  
Single File ◽  
Fast Transport ◽  
Single File Transport

Breakdown of the collective single-file behavior leads to ultra-fast transport of a simple liquid.

scholarly journals Unidirectional Single-File Transport of Full-Length Proteins Through a Nanopore

2021 ◽  
Author(s):  
Luning Yu ◽  
Xinqi Kang ◽  
Fanjun Li ◽  
Behzad Mehrafrooz ◽  
Amr Makhamreh ◽  
...  
Keyword(s):  
High Speed ◽  
Protein Transport ◽  
Ionic Current ◽  
Single Nucleotide ◽  
Osmotic Effect ◽  
Single File ◽  
Protein Fingerprinting ◽  
High Concentrations ◽  
Single File Transport ◽  
Dynamics Simulations

AbstractNanopore technology offers long, accurate sequencing of an DNA or RNA strand via enzymatic ratcheting of the strand through a nanopore in single nucleotide steps, producing stepwise modulations of the nanopore ion current. In contrast to nucleic acids, their daughter molecules, proteins, have neutral peptide backbones and side chains of varying charges. Further, proteins have stable secondary and higher order structures that obstruct protein linearization required for single file nanopore transport. Here, we describe a general approach for realizing unidirectional transport of proteins through a nanopore that neither requires the protein to be uniformly charged nor a pull from a biological enzyme. At high concentrations of guanidinium chloride, we find fulllength proteins to translocate unidirectionally through an a-hemolysin nanopore in a polymer-based membrane, provided that one of the protein ends is decorated with a short anionic peptide. Molecular dynamics simulations show that such surprisingly steady protein transport is driven by a giant electro-osmotic effect caused by binding of guanidinium cations to the inner surface of the nanopore. We show that ionic current signals produced by protein passage can be used to distinguish two biological proteins and the global orientation of the same protein (N-to-C vs. C-to-N terminus) during the nanopore transport. With the average transport rate of one amino acid per 10 μs, our method may enable direct enzyme-free protein fingerprinting or perhaps even sequencing when combined with a high-speed nanopore reader instrument.

scholarly journals Large permeabilities of hourglass nanopores: From hydrodynamics to single file transport

2014 ◽  
Vol 141 (18) ◽  
pp. 18C526 ◽  
Author(s):  
Simon Gravelle ◽  
Laurent Joly ◽  
Christophe Ybert ◽  
Lydéric Bocquet
Keyword(s):  
Single File ◽  
Single File Transport

scholarly journals Single-file transport of water through membrane channels

2018 ◽  
Vol 209 ◽  
pp. 9-33 ◽  
Author(s):  
Andreas Horner ◽  
Peter Pohl
Keyword(s):  
Potassium Channels ◽  
Water Permeability ◽  
Transport Theory ◽  
Water Channel ◽  
Gramicidin A ◽  
Membrane Channels ◽  
Short Introduction ◽  
Channel Proteins ◽  
Single File ◽  
Single File Transport

After a short introduction into the single-file transport theory, we analyze experiments in which the unitary water permeability, pf, of water channel proteins (aquaporins, AQPs), potassium channels (KcsA), and antibiotics (gramicidin-A derivatives) has been obtained. A short outline of the underlying methods is also provided.

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