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10.1016/j.bpj.2016.02.014 http://scihub22266oqcxt.onion/10.1016/j.bpj.2016.02.014 C4816718!4816718!27028643     free     free     free Deprecated: Implicit conversion from float 215.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 215.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 215.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 215.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 215.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 215.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 215.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Biophys+J 2016 ; 110 (6): 1334-45 Nephropedia Template TP {{tp|p=27028643|t=2016. Multiscale Simulations Reveal Key Aspects of the Proton Transport Mechanism in the ClC-ec1 Antiporter |pdf=|usr=}}{{27028643}} gab.com Text Multiscale Simulations Reveal Key Aspects of the Proton Transport Mechanism in the ClC-ec1 Antiporter JO: Biophys J http://www.kidney.de/pget.php?&tw=1&pmid=27028643 #FOAvip Multiscale reactive molecular dynamics simulations are used to study proton transport through the central region of ClC-ec1, a widely studied ClC transporter that enables the stoichiometric exchange of 2 Cl? ions for 1 proton (H+). It has long been known that both Cl? and proton transport occur through partially congruent pathways, and that their exchange is strictly coupled. However, the nature of this coupling and the mechanism of antiporting remain topics of debate. Here multiscale simulations have been used to characterize proton transport between E203 (Gluin) and E148 (Gluex), the internal and external intermediate proton binding sites, respectively. Free energy profiles are presented, explicitly accounting for the binding of Cl? along the central pathway, the dynamically coupled hydration changes of the central region, and conformational changes of Gluin and Gluex. We find that proton transport between Gluin and Gluex is possible in both the presence and absence of Cl? in the central binding site, although it is facilitated by the anion presence. These results support the notion that the requisite coupling between Cl? and proton transport occurs elsewhere (e.g., during proton uptake or release). In addition, proton transport is explored in the E203K mutant, which maintains proton permeation despite the substitution of a basic residue for Gluin. This collection of calculations provides for the first time, to our knowledge, a detailed picture of the proton transport mechanism in the central region of ClC-ec1 at a molecular level. Twit Text FOAVip Multiscale Simulations Reveal Key Aspects of the Proton Transport Mechanism in the ClC-ec1 Antiporter ????Biophys J http://www.kidney.de/pget.php?&tw=1&pmid=27028643 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27028643 #FOAvip English Wikipedia <ref>{{Cite pmid|27028643}}</ref> Multiscale Simulations Reveal Key Aspects of the Proton Transport Mechanism in the ClC-ec1 Antiporter #MMPMID27028643 Lee S; Swanson J; Voth G Biophys J 2016[Mar]; 110 (6): 1334-45 PMID27028643show ga Multiscale reactive molecular dynamics simulations are used to study proton transport through the central region of ClC-ec1, a widely studied ClC transporter that enables the stoichiometric exchange of 2 Cl? ions for 1 proton (H+). It has long been known that both Cl? and proton transport occur through partially congruent pathways, and that their exchange is strictly coupled. However, the nature of this coupling and the mechanism of antiporting remain topics of debate. Here multiscale simulations have been used to characterize proton transport between E203 (Gluin) and E148 (Gluex), the internal and external intermediate proton binding sites, respectively. Free energy profiles are presented, explicitly accounting for the binding of Cl? along the central pathway, the dynamically coupled hydration changes of the central region, and conformational changes of Gluin and Gluex. We find that proton transport between Gluin and Gluex is possible in both the presence and absence of Cl? in the central binding site, although it is facilitated by the anion presence. These results support the notion that the requisite coupling between Cl? and proton transport occurs elsewhere (e.g., during proton uptake or release). In addition, proton transport is explored in the E203K mutant, which maintains proton permeation despite the substitution of a basic residue for Gluin. This collection of calculations provides for the first time, to our knowledge, a detailed picture of the proton transport mechanism in the central region of ClC-ec1 at a molecular level. äMultiscale Simulations Reveal Key Aspects of the Proton Transport Mech(epmc).pdf DeepDyve Pubget Overpricing