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10.3390/ijms19020571 http://scihub22266oqcxt.onion/10.3390/ijms19020571 C5855793!5855793!29443891     free     free     free Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Int+J+Mol+Sci 2018 ; 19 (2): ä Nephropedia Template TP {{tp|p=29443891|t=2018. Conformational Dynamics and Stability of U-Shaped and S-Shaped Amyloid ? Assemblies |pdf=|usr=}}{{29443891}} gab.com Text Conformational Dynamics and Stability of U-Shaped and S-Shaped Amyloid Assemblies JO: Int J Mol Sci http://www.kidney.de/pget.php?&tw=1&pmid=29443891 #FOAvip Alzheimer?s disease is the most fatal neurodegenerative disorder characterized by the aggregation and deposition of Amyloid ? (A?) oligomers in the brain of patients. Two principal variants of A? exist in humans: A?1?40 and A?1?42. The former is the most abundant in the plaques, while the latter is the most toxic species and forms fibrils more rapidly. Interestingly, fibrils of A?1?40 peptides can only assume U-shaped conformations while A?1?42 can also arrange as S-shaped three-stranded chains, as recently discovered. As alterations in protein conformational arrangement correlate with cell toxicity and speed of disease progression, it is important to characterize, at molecular level, the conformational dynamics of amyloid fibrils. In this work, Replica Exchange Molecular Dynamics simulations were carried out to compare the conformational dynamics of U-shaped and S-shaped A?17?42 small fibrils. Our computational results provide support for the stability of the recently proposed S-shaped model due to the maximized interactions involving the C-terminal residues. On the other hand, the U-shaped motif is characterized by significant distortions resulting in a more disordered assembly. Outcomes of our work suggest that the molecular architecture of the protein aggregates might play a pivotal role in formation and conformational stability of the resulting fibrils. Twit Text FOAVip Conformational Dynamics and Stability of U-Shaped and S-Shaped Amyloid Assemblies ????Int J Mol Sci http://www.kidney.de/pget.php?&tw=1&pmid=29443891 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29443891 #FOAvip English Wikipedia <ref>{{Cite pmid|29443891}}</ref> Conformational Dynamics and Stability of U-Shaped and S-Shaped Amyloid ? Assemblies #MMPMID29443891 Grasso G; Rebella M; Muscat S; Morbiducci U; Tuszynski J; Danani A; Deriu MA Int J Mol Sci 2018[Feb]; 19 (2): ä PMID29443891show ga Alzheimer?s disease is the most fatal neurodegenerative disorder characterized by the aggregation and deposition of Amyloid ? (A?) oligomers in the brain of patients. Two principal variants of A? exist in humans: A?1?40 and A?1?42. The former is the most abundant in the plaques, while the latter is the most toxic species and forms fibrils more rapidly. Interestingly, fibrils of A?1?40 peptides can only assume U-shaped conformations while A?1?42 can also arrange as S-shaped three-stranded chains, as recently discovered. As alterations in protein conformational arrangement correlate with cell toxicity and speed of disease progression, it is important to characterize, at molecular level, the conformational dynamics of amyloid fibrils. In this work, Replica Exchange Molecular Dynamics simulations were carried out to compare the conformational dynamics of U-shaped and S-shaped A?17?42 small fibrils. Our computational results provide support for the stability of the recently proposed S-shaped model due to the maximized interactions involving the C-terminal residues. On the other hand, the U-shaped motif is characterized by significant distortions resulting in a more disordered assembly. Outcomes of our work suggest that the molecular architecture of the protein aggregates might play a pivotal role in formation and conformational stability of the resulting fibrils. äConformational Dynamics and Stability of U-Shaped and S-Shaped Amyloid(epmc).pdf DeepDyve Pubget Overpricing