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10.1073/pnas.1418155112 http://scihub22266oqcxt.onion/10.1073/pnas.1418155112 C4352815!4352815!25691742     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 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\25691742.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Proc+Natl+Acad+Sci+U+S+A 2015 ; 112 (9): 2758-63 Nephropedia Template TP {{tp|p=25691742|t=2015. Regulation and aggregation of intrinsically disordered peptides |pdf=|usr=}}{{25691742}} gab.com Text Regulation and aggregation of intrinsically disordered peptides JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=25691742 #FOAvip The microtubule-regulating protein tau is a prototypical intrinsically disordered protein (IDP) that plays an important physiological role in the human body; however, aggregates of tau are a pathological hallmark of Alzheimer?s disease. Here we demonstrate through simulations and experiments with an aggregating tau fragment that cosolvent interactions can significantly affect the balance between hydrogen bonds and salt bridge formation in IDPs, subsequently determining their preferred conformations. These subtle perturbations can dramatically shift IDPs from compact ensembles to extended ones, thereby influencing aggregate formation. These results lend considerable insight into the biophysics of the regulation and aggregation of IDPs. Twit Text FOAVip Regulation and aggregation of intrinsically disordered peptides ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=25691742 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25691742 #FOAvip English Wikipedia <ref>{{Cite pmid|25691742}}</ref> Regulation and aggregation of intrinsically disordered peptides #MMPMID25691742 Levine ZA; Larini L; LaPointe NE; Feinstein SC; Shea JE Proc Natl Acad Sci U S A 2015[Mar]; 112 (9): 2758-63 PMID25691742show ga The microtubule-regulating protein tau is a prototypical intrinsically disordered protein (IDP) that plays an important physiological role in the human body; however, aggregates of tau are a pathological hallmark of Alzheimer?s disease. Here we demonstrate through simulations and experiments with an aggregating tau fragment that cosolvent interactions can significantly affect the balance between hydrogen bonds and salt bridge formation in IDPs, subsequently determining their preferred conformations. These subtle perturbations can dramatically shift IDPs from compact ensembles to extended ones, thereby influencing aggregate formation. These results lend considerable insight into the biophysics of the regulation and aggregation of IDPs. äRegulation and aggregation of intrinsically disordered peptides (epmc).pdf DeepDyve Pubget Overpricing