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10.1021/acsnano.7b02718 http://scihub22266oqcxt.onion/10.1021/acsnano.7b02718 C5564329!5564329 !28693322     free     free     free Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\28693322 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       ACS+Nano 2017 ; 11 (7 ): 7091-7100 Nephropedia Template TP {{tp|p=28693322 |t=2017. Nanopore Sensing of Protein Folding |pdf=|usr=}}{{28693322 }} gab.com Text Nanopore Sensing of Protein Folding JO: ACS Nano http://www.kidney.de/pget.php?&tw=1&pmid=28693322 #FOAvip Single-molecule studies of protein folding hold keys to unveiling protein folding pathways and elusive intermediate folding states-attractive pharmaceutical targets. Although conventional single-molecule approaches can detect folding intermediates, they presently lack throughput and require elaborate labeling. Here, we theoretically show that measurements of ionic current through a nanopore containing a protein can report on the protein's folding state. Our all-atom molecular dynamics (MD) simulations show that the unfolding of a protein lowers the nanopore ionic current, an effect that originates from the reduction of ion mobility in proximity to a protein. Using a theoretical model, we show that the average change in ionic current produced by a folding-unfolding transition is detectable despite the orientational and conformational heterogeneity of the folded and unfolded states. By analyzing millisecond-long all-atom MD simulations of multiple protein transitions, we show that a nanopore ionic current recording can detect folding-unfolding transitions in real time and report on the structure of folding intermediates. Twit Text FOAVip Nanopore Sensing of Protein Folding ????ACS Nano http://www.kidney.de/pget.php?&tw=1&pmid=28693322 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28693322 #FOAvip English Wikipedia <ref>{{Cite pmid|28693322 }}</ref> Nanopore Sensing of Protein Folding #MMPMID28693322 Si W ; Aksimentiev A ACS Nano 2017[Jul]; 11 (7 ): 7091-7100 PMID28693322 show ga Single-molecule studies of protein folding hold keys to unveiling protein folding pathways and elusive intermediate folding states-attractive pharmaceutical targets. Although conventional single-molecule approaches can detect folding intermediates, they presently lack throughput and require elaborate labeling. Here, we theoretically show that measurements of ionic current through a nanopore containing a protein can report on the protein's folding state. Our all-atom molecular dynamics (MD) simulations show that the unfolding of a protein lowers the nanopore ionic current, an effect that originates from the reduction of ion mobility in proximity to a protein. Using a theoretical model, we show that the average change in ionic current produced by a folding-unfolding transition is detectable despite the orientational and conformational heterogeneity of the folded and unfolded states. By analyzing millisecond-long all-atom MD simulations of multiple protein transitions, we show that a nanopore ionic current recording can detect folding-unfolding transitions in real time and report on the structure of folding intermediates. |*Nanopores/ultrastructure [MESH] |*Protein Folding [MESH] |Databases, Protein [MESH] |Ion Transport [MESH] |Molecular Dynamics Simulation [MESH] |Protein Conformation [MESH] |Protein Unfolding [MESH]Nanopore Sensing of Protein Folding (epmc).pdf DeepDyve Pubget Overpricing