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10.1038/nsmb.3237 http://scihub22266oqcxt.onion/10.1038/nsmb.3237 C4937829!4937829 !27239796     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=27239796 &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\27239796 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Nat+Struct+Mol+Biol 2016 ; 23 (7 ): 691-7 Nephropedia Template TP {{tp|p=27239796 |t=2016. Visualizing chaperone-assisted protein folding |pdf=|usr=}}{{27239796 }} gab.com Text Visualizing chaperone-assisted protein folding JO: Nat Struct Mol Biol http://www.kidney.de/pget.php?&tw=1&pmid=27239796 #FOAvip Challenges in determining the structures of heterogeneous and dynamic protein complexes have greatly hampered past efforts to obtain a mechanistic understanding of many important biological processes. One such process is chaperone-assisted protein folding. Obtaining structural ensembles of chaperone-substrate complexes would ultimately reveal how chaperones help proteins fold into their native state. To address this problem, we devised a new structural biology approach based on X-ray crystallography, termed residual electron and anomalous density (READ). READ enabled us to visualize even sparsely populated conformations of the substrate protein immunity protein 7 (Im7) in complex with the Escherichia coli chaperone Spy, and to capture a series of snapshots depicting the various folding states of Im7 bound to Spy. The ensemble shows that Spy-associated Im7 samples conformations ranging from unfolded to partially folded to native-like states and reveals how a substrate can explore its folding landscape while being bound to a chaperone. Twit Text FOAVip Visualizing chaperone-assisted protein folding ????Nat Struct Mol Biol http://www.kidney.de/pget.php?&tw=1&pmid=27239796 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27239796 #FOAvip English Wikipedia <ref>{{Cite pmid|27239796 }}</ref> Visualizing chaperone-assisted protein folding #MMPMID27239796 Horowitz S ; Salmon L ; Koldewey P ; Ahlstrom LS ; Martin R ; Quan S ; Afonine PV ; van den Bedem H ; Wang L ; Xu Q ; Trievel RC ; Brooks CL 3rd ; Bardwell JC Nat Struct Mol Biol 2016[Jul]; 23 (7 ): 691-7 PMID27239796 show ga Challenges in determining the structures of heterogeneous and dynamic protein complexes have greatly hampered past efforts to obtain a mechanistic understanding of many important biological processes. One such process is chaperone-assisted protein folding. Obtaining structural ensembles of chaperone-substrate complexes would ultimately reveal how chaperones help proteins fold into their native state. To address this problem, we devised a new structural biology approach based on X-ray crystallography, termed residual electron and anomalous density (READ). READ enabled us to visualize even sparsely populated conformations of the substrate protein immunity protein 7 (Im7) in complex with the Escherichia coli chaperone Spy, and to capture a series of snapshots depicting the various folding states of Im7 bound to Spy. The ensemble shows that Spy-associated Im7 samples conformations ranging from unfolded to partially folded to native-like states and reveals how a substrate can explore its folding landscape while being bound to a chaperone. |*Protein Folding [MESH] |Amino Acid Sequence [MESH] |Binding Sites [MESH] |Carrier Proteins/*chemistry/genetics/metabolism [MESH] |Crystallography, X-Ray/methods [MESH] |Escherichia coli Proteins/*chemistry/genetics/metabolism [MESH] |Escherichia coli/genetics/*metabolism [MESH] |Gene Expression [MESH] |Kinetics [MESH] |Molecular Dynamics Simulation [MESH] |Periplasmic Proteins/*chemistry/genetics/metabolism [MESH] |Protein Binding [MESH] |Protein Interaction Domains and Motifs [MESH] |Protein Structure, Secondary [MESH] |Recombinant Proteins/chemistry/genetics/metabolism [MESH]Visualizing chaperone-assisted protein folding (epmc).pdf DeepDyve Pubget Overpricing