Ion Transport in Confined Geometries below the Nanoscale: Access Resistance Dominates Protein Channel Conductance in Diluted Solutions

ACS Nano ◽  
2017 ◽  
Vol 11 (10) ◽  
pp. 10392-10400 ◽  
Author(s):  
Antonio Alcaraz ◽  
M. Lidón López ◽  
María Queralt-Martín ◽  
Vicente M. Aguilella
2016 ◽  
Vol 148 (4) ◽  
pp. 277-291 ◽  
Author(s):  
David Naranjo ◽  
Hans Moldenhauer ◽  
Matías Pincuntureo ◽  
Ignacio Díaz-Franulic

Ion channels are membrane proteins that mediate efficient ion transport across the hydrophobic core of cell membranes, an unlikely process in their absence. K+ channels discriminate K+ over cations with similar radii with extraordinary selectivity and display a wide diversity of ion transport rates, covering differences of two orders of magnitude in unitary conductance. The pore domains of large- and small-conductance K+ channels share a general architectural design comprising a conserved narrow selectivity filter, which forms intimate interactions with permeant ions, flanked by two wider vestibules toward the internal and external openings. In large-conductance K+ channels, the inner vestibule is wide, whereas in small-conductance channels it is narrow. Here we raise the idea that the physical dimensions of the hydrophobic internal vestibule limit ion transport in K+ channels, accounting for their diversity in unitary conductance.


2001 ◽  
Vol 120 (5) ◽  
pp. A532-A532
Author(s):  
R LARSEN ◽  
M HANSEN ◽  
N BINSLEV ◽  
A MERTZNIELSEN
Keyword(s):  

Author(s):  
Tatsuhiko Sato ◽  
Koji Niita ◽  
Norihiro Matsuda ◽  
Shintaro Hashimoto ◽  
Yosuke Iwamoto ◽  
...  

Pneumologie ◽  
2016 ◽  
Vol 70 (07) ◽  
Author(s):  
JJ Salomon ◽  
T Albrecht ◽  
H Scheuermann ◽  
I Baumann ◽  
MA Mall

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