scholarly journals Secretin PulD: Association with pilot PulS, structure, and ion-conducting channel formation

1999 ◽  
Vol 96 (14) ◽  
pp. 8173-8177 ◽  
Author(s):  
N. Nouwen ◽  
N. Ranson ◽  
H. Saibil ◽  
B. Wolpensinger ◽  
A. Engel ◽  
...  
RSC Advances ◽  
2016 ◽  
Vol 6 (99) ◽  
pp. 97338-97345 ◽  
Author(s):  
Weili Li ◽  
Zhengbao Zhu ◽  
Wenjun Shen ◽  
Jijun Tang ◽  
Gang Yang ◽  
...  

A novel composite gel polymer electrolyte (CGPE) was prepared by doping ionomer-modified-graphene (IMGO) into poly(vinylidenefluoride) with a phase separation technique. IMGO can enhance the properties of CGPE due to the effect of the ion-conducting channel.


2014 ◽  
Vol 70 (a1) ◽  
pp. C634-C634
Author(s):  
Katharina Fromm ◽  
Aurélien Crochet ◽  
Cyrille Dagri ◽  
Yvens Chérémond

"Crown ethers, such as dibenzo-18-crown-6 (DB18C6) are in principle perfect building blocks to be stacked on top of each other for one-dimensional (1D) channel formation. However, in the more than 1000 publications on crown ethers in the solid state, only one case was of channel formation described, but not as main focus of research.[1] We now present a way to systematically induce the stacking of DB18C6 with the help of polyhalides, which play the roles of scaffolds via halogen bonding.[2] These compounds can be considered as ""supramolecular straws"". Using for example potassium as couter ion for triiodide for example, we obtained a solid which contains three differently filled, parallel channels in the solid state, which are arranged between the polyhalide anions. Exchanging potassium with sodium by immersion of a single crystal into NaOH solution leads to a single-crystal-to-single-crystal transformation into a compound with two channel types. This transition from a system crystallizing initially in the P2-space group to yield a compound in Pccn is only possible under these very special conditions. We will further present how the ion transport through these channels can be quantified and which process is involved in ion exchange. The role of the polyhalide anions, which cannot be replaced by other linear anions, will be emphasized as well. "


2017 ◽  
Vol 9 (15) ◽  
pp. 13406-13414 ◽  
Author(s):  
Chanchal Chakraborty ◽  
Utpal Rana ◽  
Rakesh K. Pandey ◽  
Satoshi Moriyama ◽  
Masayoshi Higuchi

1998 ◽  
Vol 112 (3) ◽  
pp. 317-324 ◽  
Author(s):  
Lisa Senzel ◽  
Paul D. Huynh ◽  
Karen S. Jakes ◽  
R. John Collier ◽  
Alan Finkelstein

The T domain of diphtheria toxin, which extends from residue 202 to 378, causes the translocation of the catalytic A fragment (residues 1–201) across endosomal membranes and also forms ion-conducting channels in planar phospholipid bilayers. The carboxy terminal 57-amino acid segment (322–378) in the T domain is all that is required to form these channels, but its ability to do so is greatly augmented by the portion of the T domain upstream from this. In this work, we show that in association with channel formation by the T domain, its NH2 terminus, as well as some or all of the adjacent hydrophilic 63 amino acid segment, cross the lipid bilayer. The phenomenon that enabled us to demonstrate that the NH2-terminal region of the T domain was translocated across the membrane was the rapid closure of channels at cis negative voltages when the T domain contained a histidine tag at its NH2 terminus. The inhibition of this effect by trans nickel, and by trans streptavidin when the histidine tag sequence was biotinylated, clearly established that the histidine tag was present on the trans side of the membrane. Furthermore, the inhibition of rapid channel closure by trans trypsin, combined with mutagenesis to localize the trypsin site, indicated that some portion of the 63 amino acid NH2-terminal segment of the T domain was also translocated to the trans side of the membrane. If the NH2 terminus was forced to remain on the cis side, by streptavidin binding to the biotinylated histidine tag sequence, channel formation was severely disrupted. Thus, normal channel formation by the T domain requires that its NH2 terminus be translocated across the membrane from the cis to the trans side, even though the NH2 terminus is >100 residues removed from the channel-forming part of the molecule.


2009 ◽  
Vol 105 (2) ◽  
pp. 024514 ◽  
Author(s):  
Yan Liang ◽  
C. Daniel Frisbie ◽  
Hsiu-Chuang Chang ◽  
P. Paul Ruden

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