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10.1016/j.cell.2016.05.054 http://scihub22266oqcxt.onion/10.1016/j.cell.2016.05.054 C4947014!4947014 !27293188     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=27293188 &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 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\27293188 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Cell 2016 ; 166 (2 ): 369-379 Nephropedia Template TP {{tp|p=27293188 |t=2016. Forces Driving Chaperone Action |pdf=|usr=}}{{27293188 }} gab.com Text Forces Driving Chaperone Action JO: Cell http://www.kidney.de/pget.php?&tw=1&pmid=27293188 #FOAvip It is still unclear what molecular forces drive chaperone-mediated protein folding. Here, we obtain a detailed mechanistic understanding of the forces that dictate the four key steps of chaperone-client interaction: initial binding, complex stabilization, folding, and release. Contrary to the common belief that chaperones recognize unfolding intermediates by their hydrophobic nature, we discover that the model chaperone Spy uses long-range electrostatic interactions to rapidly bind to its unfolded client protein Im7. Short-range hydrophobic interactions follow, which serve to stabilize the complex. Hydrophobic collapse of the client protein then drives its folding. By burying hydrophobic residues in its core, the client's affinity to Spy decreases, which causes client release. By allowing the client to fold itself, Spy circumvents the need for client-specific folding instructions. This mechanism might help explain how chaperones can facilitate the folding of various unrelated proteins. Twit Text FOAVip Forces Driving Chaperone Action ????Cell http://www.kidney.de/pget.php?&tw=1&pmid=27293188 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27293188 #FOAvip English Wikipedia <ref>{{Cite pmid|27293188 }}</ref> Forces Driving Chaperone Action #MMPMID27293188 Koldewey P ; Stull F ; Horowitz S ; Martin R ; Bardwell JCA Cell 2016[Jul]; 166 (2 ): 369-379 PMID27293188 show ga It is still unclear what molecular forces drive chaperone-mediated protein folding. Here, we obtain a detailed mechanistic understanding of the forces that dictate the four key steps of chaperone-client interaction: initial binding, complex stabilization, folding, and release. Contrary to the common belief that chaperones recognize unfolding intermediates by their hydrophobic nature, we discover that the model chaperone Spy uses long-range electrostatic interactions to rapidly bind to its unfolded client protein Im7. Short-range hydrophobic interactions follow, which serve to stabilize the complex. Hydrophobic collapse of the client protein then drives its folding. By burying hydrophobic residues in its core, the client's affinity to Spy decreases, which causes client release. By allowing the client to fold itself, Spy circumvents the need for client-specific folding instructions. This mechanism might help explain how chaperones can facilitate the folding of various unrelated proteins. |*Protein Folding [MESH] |Carrier Proteins/*chemistry/metabolism [MESH] |Entropy [MESH] |Escherichia coli Proteins/*chemistry/*metabolism [MESH] |Escherichia coli/*metabolism [MESH] |Hydrophobic and Hydrophilic Interactions [MESH] |Molecular Chaperones/*metabolism [MESH] |Periplasm/chemistry [MESH] |Periplasmic Proteins/*metabolism [MESH]Forces Driving Chaperone Action (epmc).pdf DeepDyve Pubget Overpricing