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10.1016/j.celrep.2015.07.065 http://scihub22266oqcxt.onion/10.1016/j.celrep.2015.07.065 C4571824!4571824 !26321634     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\26321634 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Cell+Rep 2015 ; 12 (10 ): 1533-40 Nephropedia Template TP {{tp|p=26321634 |t=2015. Cotranslational Protein Folding inside the Ribosome Exit Tunnel |pdf=|usr=}}{{26321634 }} gab.com Text Cotranslational Protein Folding inside the Ribosome Exit Tunnel JO: Cell Rep http://www.kidney.de/pget.php?&tw=1&pmid=26321634 #FOAvip At what point during translation do proteins fold? It is well established that proteins can fold cotranslationally outside the ribosome exit tunnel, whereas studies of folding inside the exit tunnel have so far detected only the formation of helical secondary structure and collapsed or partially structured folding intermediates. Here, using a combination of cotranslational nascent chain force measurements, inter-subunit fluorescence resonance energy transfer studies on single translating ribosomes, molecular dynamics simulations, and cryoelectron microscopy, we show that a small zinc-finger domain protein can fold deep inside the vestibule of the ribosome exit tunnel. Thus, for small protein domains, the ribosome itself can provide the kind of sheltered folding environment that chaperones provide for larger proteins. Twit Text FOAVip Cotranslational Protein Folding inside the Ribosome Exit Tunnel ????Cell Rep http://www.kidney.de/pget.php?&tw=1&pmid=26321634 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26321634 #FOAvip English Wikipedia <ref>{{Cite pmid|26321634 }}</ref> Cotranslational Protein Folding inside the Ribosome Exit Tunnel #MMPMID26321634 Nilsson OB ; Hedman R ; Marino J ; Wickles S ; Bischoff L ; Johansson M ; Müller-Lucks A ; Trovato F ; Puglisi JD ; O'Brien EP ; Beckmann R ; von Heijne G Cell Rep 2015[Sep]; 12 (10 ): 1533-40 PMID26321634 show ga At what point during translation do proteins fold? It is well established that proteins can fold cotranslationally outside the ribosome exit tunnel, whereas studies of folding inside the exit tunnel have so far detected only the formation of helical secondary structure and collapsed or partially structured folding intermediates. Here, using a combination of cotranslational nascent chain force measurements, inter-subunit fluorescence resonance energy transfer studies on single translating ribosomes, molecular dynamics simulations, and cryoelectron microscopy, we show that a small zinc-finger domain protein can fold deep inside the vestibule of the ribosome exit tunnel. Thus, for small protein domains, the ribosome itself can provide the kind of sheltered folding environment that chaperones provide for larger proteins. |*Protein Folding [MESH] |Cryoelectron Microscopy [MESH] |DNA-Binding Proteins/biosynthesis/*chemistry/genetics [MESH] |Escherichia coli [MESH] |Escherichia coli Proteins/biosynthesis/chemistry/genetics [MESH] |Fungal Proteins/biosynthesis/*chemistry/genetics [MESH] |Molecular Dynamics Simulation [MESH] |Protein Biosynthesis [MESH] |Protein Structure, Tertiary [MESH] |Ribosomes/chemistry [MESH] |Thermodynamics [MESH] |Transcription Factors/biosynthesis/chemistry/genetics [MESH]Cotranslational Protein Folding inside the Ribosome Exit Tunnel (epmc).pdf DeepDyve Pubget Overpricing