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10.1021/ja5049434 http://scihub22266oqcxt.onion/10.1021/ja5049434 C5104671!5104671 !25056406     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=25056406 &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 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 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\25056406 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       J+Am+Chem+Soc 2014 ; 136 (32 ): 11420-7 Nephropedia Template TP {{tp|p=25056406 |t=2014. General mechanism of two-state protein folding kinetics |pdf=|usr=}}{{25056406 }} gab.com Text General mechanism of two-state protein folding kinetics JO: J Am Chem Soc http://www.kidney.de/pget.php?&tw=1&pmid=25056406 #FOAvip We describe here a general model of the kinetic mechanism of protein folding. In the Foldon Funnel Model, proteins fold in units of secondary structures, which form sequentially along the folding pathway, stabilized by tertiary interactions. The model predicts that the free energy landscape has a volcano shape, rather than a simple funnel, that folding is two-state (single-exponential) when secondary structures are intrinsically unstable, and that each structure along the folding path is a transition state for the previous structure. It shows how sequential pathways are consistent with multiple stochastic routes on funnel landscapes, and it gives good agreement with the 9 order of magnitude dependence of folding rates on protein size for a set of 93 proteins, at the same time it is consistent with the near independence of folding equilibrium constant on size. This model gives estimates of folding rates of proteomes, leading to a median folding time in Escherichia coli of about 5 s. Twit Text FOAVip General mechanism of two-state protein folding kinetics ????J Am Chem Soc http://www.kidney.de/pget.php?&tw=1&pmid=25056406 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25056406 #FOAvip English Wikipedia <ref>{{Cite pmid|25056406 }}</ref> General mechanism of two-state protein folding kinetics #MMPMID25056406 Rollins GC ; Dill KA J Am Chem Soc 2014[Aug]; 136 (32 ): 11420-7 PMID25056406 show ga We describe here a general model of the kinetic mechanism of protein folding. In the Foldon Funnel Model, proteins fold in units of secondary structures, which form sequentially along the folding pathway, stabilized by tertiary interactions. The model predicts that the free energy landscape has a volcano shape, rather than a simple funnel, that folding is two-state (single-exponential) when secondary structures are intrinsically unstable, and that each structure along the folding path is a transition state for the previous structure. It shows how sequential pathways are consistent with multiple stochastic routes on funnel landscapes, and it gives good agreement with the 9 order of magnitude dependence of folding rates on protein size for a set of 93 proteins, at the same time it is consistent with the near independence of folding equilibrium constant on size. This model gives estimates of folding rates of proteomes, leading to a median folding time in Escherichia coli of about 5 s. |*Protein Folding [MESH] |Anisotropy [MESH] |Biopolymers/*chemistry [MESH] |Camphor/*chemistry [MESH] |Deuterium Oxide/chemistry [MESH] |Graphite/*chemistry [MESH] |Kinetics [MESH] |Magnetic Resonance Spectroscopy [MESH] |Molecular Weight [MESH] |Organic Chemicals [MESH] |Oxides/*chemistry [MESH] |Proline/chemistry [MESH] |Proteins/*chemistry [MESH] |Solutions [MESH] |Solvents/chemistry [MESH]General mechanism of two-state protein folding kinetics (epmc).pdf DeepDyve Pubget Overpricing