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10.2142/biophysico.13.0_263 http://scihub22266oqcxt.onion/10.2142/biophysico.13.0_263 C5221509!5221509!28409079     free     free     free 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 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 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Biophys+Physicobiol 2016 ; 13 (ä): 263-79 Nephropedia Template TP {{tp|p=28409079|t=2016. Characterization of protein folding by a ?-value calculation with a statistical-mechanical model |pdf=|usr=}}{{28409079}} gab.com Text Characterization of protein folding by a -value calculation with a statistical-mechanical model JO: Biophys Physicobiol http://www.kidney.de/pget.php?&tw=1&pmid=28409079 #FOAvip The ?-value analysis approach provides information about transition-state structures along the folding pathway of a protein by measuring the effects of an amino acid mutation on folding kinetics. Here we compared the theoretically calculated ? values of 27 proteins with their experimentally observed ? values; the theoretical values were calculated using a simple statistical-mechanical model of protein folding. The theoretically calculated ? values reflected the corresponding experimentally observed ? values with reasonable accuracy for many of the proteins, but not for all. The correlation between the theoretically calculated and experimentally observed ? values strongly depends on whether the protein-folding mechanism assumed in the model holds true in real proteins. In other words, the correlation coefficient can be expected to illuminate the folding mechanisms of proteins, providing the answer to the question of which model more accurately describes protein folding: the framework model or the nucleation-condensation model. In addition, we tried to characterize protein folding with respect to various properties of each protein apart from the size and fold class, such as the free-energy profile, contact-order profile, and sensitivity to the parameters used in the ?-value calculation. The results showed that any one of these properties alone was not enough to explain protein folding, although each one played a significant role in it. We have confirmed the importance of characterizing protein folding from various perspectives. Our findings have also highlighted that protein folding is highly variable and unique across different proteins, and this should be considered while pursuing a unified theory of protein folding. Twit Text FOAVip Characterization of protein folding by a -value calculation with a statistical-mechanical model ????Biophys Physicobiol http://www.kidney.de/pget.php?&tw=1&pmid=28409079 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28409079 #FOAvip English Wikipedia <ref>{{Cite pmid|28409079}}</ref> Characterization of protein folding by a ?-value calculation with a statistical-mechanical model #MMPMID28409079 Wako H; Abe H Biophys Physicobiol 2016[]; 13 (ä): 263-79 PMID28409079show ga The ?-value analysis approach provides information about transition-state structures along the folding pathway of a protein by measuring the effects of an amino acid mutation on folding kinetics. Here we compared the theoretically calculated ? values of 27 proteins with their experimentally observed ? values; the theoretical values were calculated using a simple statistical-mechanical model of protein folding. The theoretically calculated ? values reflected the corresponding experimentally observed ? values with reasonable accuracy for many of the proteins, but not for all. The correlation between the theoretically calculated and experimentally observed ? values strongly depends on whether the protein-folding mechanism assumed in the model holds true in real proteins. In other words, the correlation coefficient can be expected to illuminate the folding mechanisms of proteins, providing the answer to the question of which model more accurately describes protein folding: the framework model or the nucleation-condensation model. In addition, we tried to characterize protein folding with respect to various properties of each protein apart from the size and fold class, such as the free-energy profile, contact-order profile, and sensitivity to the parameters used in the ?-value calculation. The results showed that any one of these properties alone was not enough to explain protein folding, although each one played a significant role in it. We have confirmed the importance of characterizing protein folding from various perspectives. Our findings have also highlighted that protein folding is highly variable and unique across different proteins, and this should be considered while pursuing a unified theory of protein folding. äCharacterization of protein folding by a ?-value calculation with a st(epmc).pdf DeepDyve Pubget Overpricing