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10.4161/chan.28665 http://scihub22266oqcxt.onion/10.4161/chan.28665 C4203746!4203746!24755912     free     free     free Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Channels+(Austin) 2014 ; 8 (3): 180-92 Nephropedia Template TP {{tp|p=24755912|t=2014. Proton channel models: Filling the gap between experimental data and the structural rationale |pdf=|usr=}}{{24755912}} gab.com Text Proton channel models: Filling the gap between experimental data and the structural rationale JO: Channels (Austin) http://www.kidney.de/pget.php?&tw=1&pmid=24755912 #FOAvip Voltage-gated proton channels are integral membrane proteins with the capacity to permeate elementary particles in a voltage and pH dependent manner. These proteins have been found in several species and are involved in various physiological processes. Although their primary topology is known, lack of details regarding their structures in the open conformation has limited analyses toward a deeper understanding of the molecular determinants of their function and regulation. Consequently, the function-structure relationships have been inferred based on homology models. In the present work, we review the existing proton channel models, their assumptions, predictions and the experimental facts that support them. Modeling proton channels is not a trivial task due to the lack of a close homolog template. Hence, there are important differences between published models. This work attempts to critically review existing proton channel models toward the aim of contributing to a better understanding of the structural features of these proteins. Twit Text FOAVip Proton channel models: Filling the gap between experimental data and the structural rationale ????Channels (Austin) http://www.kidney.de/pget.php?&tw=1&pmid=24755912 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=24755912 #FOAvip English Wikipedia <ref>{{Cite pmid|24755912}}</ref> Proton channel models: Filling the gap between experimental data and the structural rationale #MMPMID24755912 Pupo A; Baez-Nieto D; Martínez A; Latorre R; González C Channels (Austin) 2014[May]; 8 (3): 180-92 PMID24755912show ga Voltage-gated proton channels are integral membrane proteins with the capacity to permeate elementary particles in a voltage and pH dependent manner. These proteins have been found in several species and are involved in various physiological processes. Although their primary topology is known, lack of details regarding their structures in the open conformation has limited analyses toward a deeper understanding of the molecular determinants of their function and regulation. Consequently, the function-structure relationships have been inferred based on homology models. In the present work, we review the existing proton channel models, their assumptions, predictions and the experimental facts that support them. Modeling proton channels is not a trivial task due to the lack of a close homolog template. Hence, there are important differences between published models. This work attempts to critically review existing proton channel models toward the aim of contributing to a better understanding of the structural features of these proteins. äProton channel models: Filling the gap between experimental data and t(epmc).pdf DeepDyve Pubget Overpricing