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10.1038/srep33156 http://scihub22266oqcxt.onion/10.1038/srep33156 C5018807!5018807 !27616019     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=27616019 &cmd=llinks): Failed to open stream: HTTP request failed! 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An Atomistic View of Amyloidogenic Self-assembly: Structure and Dynamics of Heterogeneous Conformational States in the Pre-nucleation Phase |pdf=|usr=}}{{27616019 }} gab.com Text An Atomistic View of Amyloidogenic Self-assembly: Structure and Dynamics of Heterogeneous Conformational States in the Pre-nucleation Phase JO: Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=27616019 #FOAvip The formation of well-defined filamentous amyloid structures involves a polydisperse collection of oligomeric states for which relatively little is known in terms of structural organization. Here we use extensive, unbiased explicit solvent molecular dynamics (MD) simulations to investigate the structural and dynamical features of oligomeric aggregates formed by a number of highly amyloidogenic peptides at atomistic resolution on the ?s time scale. A consensus approach has been adopted to analyse the simulations in multiple force fields, yielding an in-depth characterization of pre-fibrillar oligomers and their global and local structure properties. A collision cross section analysis revealed structurally heterogeneous aggregate ensembles for the individual oligomeric states that lack a single defined quaternary structure during the pre-nucleation phase. To gain insight into the conformational space sampled in early aggregates, we probed their substructure and found emerging ?-sheet subunit layers and a multitude of ordered intermolecular ?-structure motifs with growing aggregate size. Among those, anti-parallel out-of-register ?-strands compatible with toxic ?-barrel oligomers were particularly prevalent already in smaller aggregates and formed prior to ordered fibrillar structure elements. Notably, also distinct fibril-like conformations emerged in the oligomeric state and underscore the notion that pre-nucleated oligomers serve as a critical intermediate step on-pathway to fibrils. Twit Text FOAVip An Atomistic View of Amyloidogenic Self-assembly: Structure and Dynamics of Heterogeneous Conformational States in the Pre-nucleation Phase ????Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=27616019 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27616019 #FOAvip English Wikipedia <ref>{{Cite pmid|27616019 }}</ref> An Atomistic View of Amyloidogenic Self-assembly: Structure and Dynamics of Heterogeneous Conformational States in the Pre-nucleation Phase #MMPMID27616019 Matthes D ; Gapsys V ; Brennecke JT ; de Groot BL Sci Rep 2016[Sep]; 6 (ä): 33156 PMID27616019 show ga The formation of well-defined filamentous amyloid structures involves a polydisperse collection of oligomeric states for which relatively little is known in terms of structural organization. Here we use extensive, unbiased explicit solvent molecular dynamics (MD) simulations to investigate the structural and dynamical features of oligomeric aggregates formed by a number of highly amyloidogenic peptides at atomistic resolution on the ?s time scale. A consensus approach has been adopted to analyse the simulations in multiple force fields, yielding an in-depth characterization of pre-fibrillar oligomers and their global and local structure properties. A collision cross section analysis revealed structurally heterogeneous aggregate ensembles for the individual oligomeric states that lack a single defined quaternary structure during the pre-nucleation phase. To gain insight into the conformational space sampled in early aggregates, we probed their substructure and found emerging ?-sheet subunit layers and a multitude of ordered intermolecular ?-structure motifs with growing aggregate size. Among those, anti-parallel out-of-register ?-strands compatible with toxic ?-barrel oligomers were particularly prevalent already in smaller aggregates and formed prior to ordered fibrillar structure elements. Notably, also distinct fibril-like conformations emerged in the oligomeric state and underscore the notion that pre-nucleated oligomers serve as a critical intermediate step on-pathway to fibrils. |*Molecular Dynamics Simulation [MESH] |Amino Acid Sequence [MESH] |Amyloidogenic Proteins/*chemistry [MESH] |Hydrogen Bonding [MESH] |Hydrophobic and Hydrophilic Interactions [MESH] |Protein Aggregates [MESH] |Protein Conformation, beta-Strand [MESH] |Protein Multimerization [MESH] |Protein Structure, Quaternary [MESH]An Atomistic View of Amyloidogenic Self-assembly: Structure and Dynami(epmc).pdf DeepDyve Pubget Overpricing