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10.1073/pnas.1418155112 http://scihub22266oqcxt.onion/10.1073/pnas.1418155112 C4352815!4352815 !25691742     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=25691742 &cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 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 Intrinsically disordered proteins (IDPs) are a unique class of proteins that have no stable native structure, a feature that allows them to adopt a wide variety of extended and compact conformations that facilitate a large number of vital physiological functions. One of the most well-known IDPs is the microtubule-associated tau protein, which regulates microtubule growth in the nervous system. However, dysfunctions in tau can lead to tau oligomerization, fibril formation, and neurodegenerative disease, including Alzheimer's disease. Using a combination of simulations and experiments, we explore the role of osmolytes in regulating the conformation and aggregation propensities of the R2/wt peptide, a fragment of tau containing the aggregating paired helical filament (PHF6*). We show that the osmolytes urea and trimethylamine N-oxide (TMAO) shift the population of IDP monomer structures, but that no new conformational ensembles emerge. Although urea halts aggregation, TMAO promotes the formation of compact oligomers (including helical oligomers) through a newly proposed mechanism of redistribution of water around the perimeter of the peptide. We put forth a "superposition of ensembles" hypothesis to rationalize the mechanism by which IDP structure and aggregation is regulated in the cell. 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 PMID25691742 show ga Intrinsically disordered proteins (IDPs) are a unique class of proteins that have no stable native structure, a feature that allows them to adopt a wide variety of extended and compact conformations that facilitate a large number of vital physiological functions. One of the most well-known IDPs is the microtubule-associated tau protein, which regulates microtubule growth in the nervous system. However, dysfunctions in tau can lead to tau oligomerization, fibril formation, and neurodegenerative disease, including Alzheimer's disease. Using a combination of simulations and experiments, we explore the role of osmolytes in regulating the conformation and aggregation propensities of the R2/wt peptide, a fragment of tau containing the aggregating paired helical filament (PHF6*). We show that the osmolytes urea and trimethylamine N-oxide (TMAO) shift the population of IDP monomer structures, but that no new conformational ensembles emerge. Although urea halts aggregation, TMAO promotes the formation of compact oligomers (including helical oligomers) through a newly proposed mechanism of redistribution of water around the perimeter of the peptide. We put forth a "superposition of ensembles" hypothesis to rationalize the mechanism by which IDP structure and aggregation is regulated in the cell. |*Molecular Dynamics Simulation [MESH] |*Protein Aggregation, Pathological [MESH] |Humans [MESH] |Methylamines/chemistry [MESH] |Peptides/*chemistry [MESH] |Protein Structure, Secondary [MESH] |Urea/chemistry [MESH]Regulation and aggregation of intrinsically disordered peptides (epmc).pdf DeepDyve Pubget Overpricing