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10.1073/pnas.1613331114 http://scihub22266oqcxt.onion/10.1073/pnas.1613331114 C5358400!5358400!28265078     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       Proc+Natl+Acad+Sci+U+S+A 2017 ; 114 (11): 2928-33 Nephropedia Template TP {{tp|p=28265078|t=2017. Knowledge-based entropies improve the identification of native protein structures |pdf=|usr=}}{{28265078}} gab.com Text Knowledge-based entropies improve the identification of native protein structures JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=28265078 #FOAvip The protein folding process is dictated by the free-energy landscape and thus accurate prediction of the native structures of proteins requires reliable estimates of free energies. Computed energies of proteins are at present significantly more reliable than entropies. In this work, we introduce an innovative method to estimate the local conformational entropies of protein structures by using statistical data from observed amino acid contact changes during conformational transitions within a set of diverse protein structures. Combining these new entropies with cooperative potential energy functions yields significant gains in the ability to distinguish between native structures of proteins and their nonnative decoys. Twit Text FOAVip Knowledge-based entropies improve the identification of native protein structures ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=28265078 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28265078 #FOAvip English Wikipedia <ref>{{Cite pmid|28265078}}</ref> Knowledge-based entropies improve the identification of native protein structures #MMPMID28265078 Sankar K; Jia K; Jernigan RL Proc Natl Acad Sci U S A 2017[Mar]; 114 (11): 2928-33 PMID28265078show ga The protein folding process is dictated by the free-energy landscape and thus accurate prediction of the native structures of proteins requires reliable estimates of free energies. Computed energies of proteins are at present significantly more reliable than entropies. In this work, we introduce an innovative method to estimate the local conformational entropies of protein structures by using statistical data from observed amino acid contact changes during conformational transitions within a set of diverse protein structures. Combining these new entropies with cooperative potential energy functions yields significant gains in the ability to distinguish between native structures of proteins and their nonnative decoys. äKnowledge-based entropies improve the identification of native protein(epmc).pdf DeepDyve Pubget Overpricing