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10.1016/j.sbi.2016.10.006 http://scihub22266oqcxt.onion/10.1016/j.sbi.2016.10.006 C5397379!5397379!27771543     free     free     free Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Curr+Opin+Struct+Biol 2017 ; 43 (ä): 28-37 Nephropedia Template TP {{tp|p=27771543|t=2017. Protein Folding, Binding, and Droplet Formation in Cell-Like Conditions |pdf=|usr=}}{{27771543}} gab.com Text Protein Folding, Binding, and Droplet Formation in Cell-Like Conditions JO: Curr Opin Struct Biol http://www.kidney.de/pget.php?&tw=1&pmid=27771543 #FOAvip The many bystander macromolecules in the crowded cellular environments present both steric repulsion and weak attraction to proteins undergoing folding or binding and hence impact the thermodynamic and kinetic properties of these processes. The weak not nonrandom binding with bystander macromolecules may facilitate subcellular localization and biological function. Weak binding also leads to the emergence of a protein-rich, droplet phase, which has been implicated in regulating a variety of cellular functions. All these important problems can now be addressed by realistic modeling of intermolecular interactions. Configurational sampling of concentrated protein solutions is an ongoing challenge. Twit Text FOAVip Protein Folding, Binding, and Droplet Formation in Cell-Like Conditions ????Curr Opin Struct Biol http://www.kidney.de/pget.php?&tw=1&pmid=27771543 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27771543 #FOAvip English Wikipedia <ref>{{Cite pmid|27771543}}</ref> Protein Folding, Binding, and Droplet Formation in Cell-Like Conditions #MMPMID27771543 Qin S; Zhou HX Curr Opin Struct Biol 2017[Apr]; 43 (ä): 28-37 PMID27771543show ga The many bystander macromolecules in the crowded cellular environments present both steric repulsion and weak attraction to proteins undergoing folding or binding and hence impact the thermodynamic and kinetic properties of these processes. The weak not nonrandom binding with bystander macromolecules may facilitate subcellular localization and biological function. Weak binding also leads to the emergence of a protein-rich, droplet phase, which has been implicated in regulating a variety of cellular functions. All these important problems can now be addressed by realistic modeling of intermolecular interactions. Configurational sampling of concentrated protein solutions is an ongoing challenge. äProtein Folding, Binding, and Droplet Formation in Cell-Like Condition(epmc).pdf DeepDyve Pubget Overpricing