2018
DOI: 10.1039/c8fd00050f
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Positively charged residues at the channel mouth boost single-file water flow

Abstract: Positively charged residues in the vicinity of the channel entrance or exit accelerate single-file water flow.

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Cited by 41 publications
(83 citation statements)
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References 32 publications
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“…22,36,37,69,93 Even though the latter method relies on uo-rescence labeling of the channel, FCS is a very convenient, reliable and time efficient method which can be used in vivo as well as in vitro. The protein concentration in the plasma membrane of polarized or non-polarized cells, GUVs or free standing planar lipid bilayers can be directly assessed.…”
Section: G Protein Countingmentioning
confidence: 99%
“…22,36,37,69,93 Even though the latter method relies on uo-rescence labeling of the channel, FCS is a very convenient, reliable and time efficient method which can be used in vivo as well as in vitro. The protein concentration in the plasma membrane of polarized or non-polarized cells, GUVs or free standing planar lipid bilayers can be directly assessed.…”
Section: G Protein Countingmentioning
confidence: 99%
“…( 1 ), which was already published in 2015. However, the analytical solution was only applied in our work group so far to calculate p f values of AQP1, GlpF, AqpZ, KcsA 38 , AQP4 53 and hSGLT1 3 . We attribute this to the fact that the Lambert function as part of the analytical solution is not implemented in common tools for stopped-flow data analysis.…”
Section: Discussionmentioning
confidence: 99%
“…PLs and LUVs are subjected to a hyperosmotic solution in a stopped-flow apparatus (SFM-300, Bio-Logic, Claix, France) at 4 °C. As previously described 3 , 4 , 38 , 53 , we monitor the intensity of scattered light at 90° at a wavelength of 546 nm. To calculate water permeability values from light scattering we use our recently found analytical solution 38 and three common approximations 25 , 41 , 42 as well as our new approximation all based on single-exponential functions with a time constant τ where depending on different models Π is equal to c out −1 , (c out – c in,0 ) −1 , c in,0 ·c out −2 or (c in,0 + c out )/(2· c out 2 ).…”
Section: Methodsmentioning
confidence: 99%
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“…Plot of unitary water permeability of water channel proteins against the available number of hydrogen bonding sites in the single‐file region of pore walls. Adapted with permission from References . [Color figure can be viewed at wileyonlinelibrary.com]…”
Section: Mechanisms Of Water Transport Through Aquaporinsmentioning
confidence: 99%