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10.1073/pnas.1614609114 http://scihub22266oqcxt.onion/10.1073/pnas.1614609114 C5347566!5347566!28228526     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Proc+Natl+Acad+Sci+U+S+A 2017 ; 114 (10): 2479-84 Nephropedia Template TP {{tp|p=28228526|t=2017. Trimethylamine N-oxide stabilizes proteins via a distinct mechanism compared with betaine and glycine |pdf=|usr=}}{{28228526}} gab.com Text Trimethylamine N-oxide stabilizes proteins via a distinct mechanism compared with betaine and glycine JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=28228526 #FOAvip Although trimethylamine N-oxide (TMAO) is perhaps the quintessential protein-stabilizing osmolyte, its mechanism of action has long remained elusive. Our study indicates that, in contrast to betaine and glycine, TMAO forms direct attractive interactions with polypeptides. This work strengthens and extends Berne?s previous conclusions, because we report results for a model polypeptide rather than a hydrophobic polymer. Our results are particularly striking, because we consider a model polypeptide that is enriched in amide groups that are believed responsible for the depletion of TMAO from unfolded proteins. Our study leads to the surprising conclusion that TMAO stabilizes folded conformations, despite interacting with unfolded conformations. We hypothesize that TMAO acts as a unique surfactant for the heterogeneous surface that emerges on protein folding. Twit Text FOAVip Trimethylamine N-oxide stabilizes proteins via a distinct mechanism compared with betaine and glycine ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=28228526 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28228526 #FOAvip English Wikipedia <ref>{{Cite pmid|28228526}}</ref> Trimethylamine N-oxide stabilizes proteins via a distinct mechanism compared with betaine and glycine #MMPMID28228526 Liao YT; Manson AC; DeLyser MR; Noid WG; Cremer PS Proc Natl Acad Sci U S A 2017[Mar]; 114 (10): 2479-84 PMID28228526show ga Although trimethylamine N-oxide (TMAO) is perhaps the quintessential protein-stabilizing osmolyte, its mechanism of action has long remained elusive. Our study indicates that, in contrast to betaine and glycine, TMAO forms direct attractive interactions with polypeptides. This work strengthens and extends Berne?s previous conclusions, because we report results for a model polypeptide rather than a hydrophobic polymer. Our results are particularly striking, because we consider a model polypeptide that is enriched in amide groups that are believed responsible for the depletion of TMAO from unfolded proteins. Our study leads to the surprising conclusion that TMAO stabilizes folded conformations, despite interacting with unfolded conformations. We hypothesize that TMAO acts as a unique surfactant for the heterogeneous surface that emerges on protein folding. äTrimethylamine N-oxide stabilizes proteins via a distinct mechanism co(epmc).pdf DeepDyve Pubget Overpricing