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10.1016/j.bpj.2016.06.031 http://scihub22266oqcxt.onion/10.1016/j.bpj.2016.06.031 C5018131!5018131 !27602721     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 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\27602721 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Biophys+J 2016 ; 111 (5 ): 925-36 Nephropedia Template TP {{tp|p=27602721 |t=2016. Structure-Based Prediction of Protein-Folding Transition Paths |pdf=|usr=}}{{27602721 }} gab.com Text Structure-Based Prediction of Protein-Folding Transition Paths JO: Biophys J http://www.kidney.de/pget.php?&tw=1&pmid=27602721 #FOAvip We propose a general theory to describe the distribution of protein-folding transition paths. We show that transition paths follow a predictable sequence of high-free-energy transient states that are separated by free-energy barriers. Each transient state corresponds to the assembly of one or more discrete, cooperative units, which are determined directly from the native structure. We show that the transition state on a folding pathway is reached when a small number of critical contacts are formed between a specific set of substructures, after which folding proceeds downhill in free energy. This approach suggests a natural resolution for distinguishing parallel folding pathways and provides a simple means to predict the rate-limiting step in a folding reaction. Our theory identifies a common folding mechanism for proteins with diverse native structures and establishes general principles for the self-assembly of polymers with specific interactions. Twit Text FOAVip Structure-Based Prediction of Protein-Folding Transition Paths ????Biophys J http://www.kidney.de/pget.php?&tw=1&pmid=27602721 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27602721 #FOAvip English Wikipedia <ref>{{Cite pmid|27602721 }}</ref> Structure-Based Prediction of Protein-Folding Transition Paths #MMPMID27602721 Jacobs WM ; Shakhnovich EI Biophys J 2016[Sep]; 111 (5 ): 925-36 PMID27602721 show ga We propose a general theory to describe the distribution of protein-folding transition paths. We show that transition paths follow a predictable sequence of high-free-energy transient states that are separated by free-energy barriers. Each transient state corresponds to the assembly of one or more discrete, cooperative units, which are determined directly from the native structure. We show that the transition state on a folding pathway is reached when a small number of critical contacts are formed between a specific set of substructures, after which folding proceeds downhill in free energy. This approach suggests a natural resolution for distinguishing parallel folding pathways and provides a simple means to predict the rate-limiting step in a folding reaction. Our theory identifies a common folding mechanism for proteins with diverse native structures and establishes general principles for the self-assembly of polymers with specific interactions. |*Models, Molecular [MESH] |*Protein Folding [MESH] |Algorithms [MESH] |Kinetics [MESH] |Protein Stability [MESH] |Structure-Activity Relationship [MESH]Structure-Based Prediction of Protein-Folding Transition Paths (epmc).pdf DeepDyve Pubget Overpricing