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10.1007/s12551-017-0262-x http://scihub22266oqcxt.onion/10.1007/s12551-017-0262-x C5380711!5380711!28424741     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Biophys+Rev 2017 ; 9 (2): 103-18 Nephropedia Template TP {{tp|p=28424741|t=2017. Catalytic robustness and torque generation of the F1-ATPase |pdf=|usr=}}{{28424741}} gab.com Text Catalytic robustness and torque generation of the F1-ATPase JO: Biophys Rev http://www.kidney.de/pget.php?&tw=1&pmid=28424741 #FOAvip The F1-ATPase is the catalytic portion of the FoF1 ATP synthase and acts as a rotary molecular motor when it hydrolyzes ATP. Two decades have passed since the single-molecule rotation assay of F1-ATPase was established. Although several fundamental issues remain elusive, basic properties of F-type ATPases as motor proteins have been well characterized, and a large part of the reaction scheme has been revealed by the combination of extensive structural, biochemical, biophysical, and theoretical studies. This review is intended to provide a concise summary of the fundamental features of F1-ATPases, by use of the well-described model F1 from the thermophilic Bacillus PS3 (TF1). In the last part of this review, we focus on the robustness of the rotary catalysis of F1-ATPase to provide a perspective on the re-designing of novel molecular machines. Twit Text FOAVip Catalytic robustness and torque generation of the F1-ATPase ????Biophys Rev http://www.kidney.de/pget.php?&tw=1&pmid=28424741 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28424741 #FOAvip English Wikipedia <ref>{{Cite pmid|28424741}}</ref> Catalytic robustness and torque generation of the F1-ATPase #MMPMID28424741 Noji H; Ueno H; McMillan DGG Biophys Rev 2017[Apr]; 9 (2): 103-18 PMID28424741show ga The F1-ATPase is the catalytic portion of the FoF1 ATP synthase and acts as a rotary molecular motor when it hydrolyzes ATP. Two decades have passed since the single-molecule rotation assay of F1-ATPase was established. Although several fundamental issues remain elusive, basic properties of F-type ATPases as motor proteins have been well characterized, and a large part of the reaction scheme has been revealed by the combination of extensive structural, biochemical, biophysical, and theoretical studies. This review is intended to provide a concise summary of the fundamental features of F1-ATPases, by use of the well-described model F1 from the thermophilic Bacillus PS3 (TF1). In the last part of this review, we focus on the robustness of the rotary catalysis of F1-ATPase to provide a perspective on the re-designing of novel molecular machines. äCatalytic robustness and torque generation of the F1-ATPase (epmc).pdf DeepDyve Pubget Overpricing