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10.1016/j.bpj.2015.01.013 http://scihub22266oqcxt.onion/10.1016/j.bpj.2015.01.013 C4375620!4375620!25762329     free     free     free Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\25762329.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Biophys+J 2015 ; 108 (5): 1176-86 Nephropedia Template TP {{tp|p=25762329|t=2015. Nucleation of Polymorphic Amyloid Fibrils |pdf=|usr=}}{{25762329}} gab.com Text Nucleation of Polymorphic Amyloid Fibrils JO: Biophys J http://www.kidney.de/pget.php?&tw=1&pmid=25762329 #FOAvip One and the same protein can self-assemble into amyloid fibrils with different morphologies. The phenomenon of fibril polymorphism is relevant biologically because different fibril polymorphs can have different toxicity, but there is no tool for predicting which polymorph forms and under what conditions. Here, we consider the nucleation of polymorphic amyloid fibrils occurring by direct polymerization of monomeric proteins into fibrils. We treat this process within the framework of our newly developed nonstandard nucleation theory, which allows prediction of the concentration dependence of the nucleation rate for different fibril polymorphs. The results highlight that the concentration dependence of the nucleation rate is closely linked with the protein solubility and a threshold monomer concentration below which fibril formation becomes biologically irrelevant. The relation between the nucleation rate, the fibril solubility, the threshold concentration, and the binding energies of the fibril building blocks within fibrils might prove a valuable tool for designing new experiments to control the formation of particular fibril polymorphs. Twit Text FOAVip Nucleation of Polymorphic Amyloid Fibrils ????Biophys J http://www.kidney.de/pget.php?&tw=1&pmid=25762329 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25762329 #FOAvip English Wikipedia <ref>{{Cite pmid|25762329}}</ref> Nucleation of Polymorphic Amyloid Fibrils #MMPMID25762329 Auer S Biophys J 2015[Mar]; 108 (5): 1176-86 PMID25762329show ga One and the same protein can self-assemble into amyloid fibrils with different morphologies. The phenomenon of fibril polymorphism is relevant biologically because different fibril polymorphs can have different toxicity, but there is no tool for predicting which polymorph forms and under what conditions. Here, we consider the nucleation of polymorphic amyloid fibrils occurring by direct polymerization of monomeric proteins into fibrils. We treat this process within the framework of our newly developed nonstandard nucleation theory, which allows prediction of the concentration dependence of the nucleation rate for different fibril polymorphs. The results highlight that the concentration dependence of the nucleation rate is closely linked with the protein solubility and a threshold monomer concentration below which fibril formation becomes biologically irrelevant. The relation between the nucleation rate, the fibril solubility, the threshold concentration, and the binding energies of the fibril building blocks within fibrils might prove a valuable tool for designing new experiments to control the formation of particular fibril polymorphs. äNucleation of Polymorphic Amyloid Fibrils (epmc).pdf DeepDyve Pubget Overpricing