Single-file transport of water through membrane channels

Faraday Discussions
Andreas Horner, Peter Pohl

Abstract

Water at interfaces governs many processes on the molecular scale from electrochemical and enzymatic reactions to protein folding. Here we focus on water transport through proteinaceous pores that are so narrow that the water molecules cannot overtake each other in the pore. 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 (scanning electrochemical microscopy, fluorescence correlation spectroscopy, measurements of vesicle light scattering) is also provided. We conclude that pf increases exponentially with a decreasing number NH of hydrogen bond donating or accepting residues in the channel wall. The variance in NH is responsible for a more than hundredfold change in pf. The dehydration penalty at the channel mouth has a smaller effect on pf. The intricate link between pf and the Gibbs activation energy barrier, ΔG‡t, for water flow suggests that conformational transitions of water channels act as a third determinant of pf.

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Citations

Sep 19, 2018·Faraday Discussions·Bing Gong
Oct 2, 2019·The Journal of Pharmacology and Experimental Therapeutics·Raul A MarinelliNorman B Javitt
Apr 30, 2020·Biotechnology Journal·Danila BoytsovPeter Pohl
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May 18, 2020·Proceedings of the National Academy of Sciences of the United States of America·Joana PaulinoTimothy A Cross
Sep 18, 2020·Science Advances·Yuhao LiAleksandr Noy
Jul 5, 2018·Faraday Discussions·Andreas HornerPeter Pohl
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Methods Mentioned

BETA
protein folding
NMR
light scattering
fluorescence correlation spectroscopy
electron microscopy
electrochemical microscopy
confocal microscopy
FCS
AFM

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