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10.1007/s12551-013-0100-8 http://scihub22266oqcxt.onion/10.1007/s12551-013-0100-8 C5425704!5425704!28510109     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=28510109&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\28510109.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Biophys+Rev 2013 ; 5 (3): 283-93 Nephropedia Template TP {{tp|p=28510109|t=2013. A new theoretical approach to biological self-assembly |pdf=|usr=}}{{28510109}} gab.com Text A new theoretical approach to biological self-assembly JO: Biophys Rev http://www.kidney.de/pget.php?&tw=1&pmid=28510109 #FOAvip Upon biological self-assembly, the number of accessible translational configurations of water in the system increases considerably, leading to a large gain in water entropy. It is important to calculate the solvation entropy of a biomolecule with a prescribed structure by accounting for the change in water?water correlations caused by solute insertion. Modeling water as a dielectric continuum is not capable of capturing the physical essence of the water entropy effect. As a reliable tool, we propose a hybrid of the angle-dependent integral equation theory combined with a multipolar water model and a morphometric approach. Using our methods wherein the water entropy effect is treated as the key factor, we can elucidate a variety of processes such as protein folding, cold, pressure, and heat denaturating of a protein, molecular recognition, ordered association of proteins such as amyloid fibril formation, and functioning of ATP-driven proteins. Twit Text FOAVip A new theoretical approach to biological self-assembly ????Biophys Rev http://www.kidney.de/pget.php?&tw=1&pmid=28510109 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28510109 #FOAvip English Wikipedia <ref>{{Cite pmid|28510109}}</ref> A new theoretical approach to biological self-assembly #MMPMID28510109 Kinoshita M Biophys Rev 2013[Sep]; 5 (3): 283-93 PMID28510109show ga Upon biological self-assembly, the number of accessible translational configurations of water in the system increases considerably, leading to a large gain in water entropy. It is important to calculate the solvation entropy of a biomolecule with a prescribed structure by accounting for the change in water?water correlations caused by solute insertion. Modeling water as a dielectric continuum is not capable of capturing the physical essence of the water entropy effect. As a reliable tool, we propose a hybrid of the angle-dependent integral equation theory combined with a multipolar water model and a morphometric approach. Using our methods wherein the water entropy effect is treated as the key factor, we can elucidate a variety of processes such as protein folding, cold, pressure, and heat denaturating of a protein, molecular recognition, ordered association of proteins such as amyloid fibril formation, and functioning of ATP-driven proteins. äA new theoretical approach to biological self-assembly (epmc).pdf DeepDyve Pubget Overpricing