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10.1073/pnas.1621227114 http://scihub22266oqcxt.onion/10.1073/pnas.1621227114 C5468600!5468600!28536196     free     free     free Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 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 (23): E4556-63 Nephropedia Template TP {{tp|p=28536196|t=2017. Physicochemical code for quinary protein interactions in Escherichia coli |pdf=|usr=}}{{28536196}} gab.com Text Physicochemical code for quinary protein interactions in Escherichia coli JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=28536196 #FOAvip This study shows that the diffusive motions of proteins in live cells are by no means without control but follow simplistic physical?chemical rules that can be quantified and optimized through surface composition. Most strikingly, human proteins are observed to stick to the ?foreign? environment of bacterial cells, whereas the bacterial analogue moves around freely. Even so, the human proteins can predictably be transformed to bacterial behavior with a few structurally benign surface mutations, and, conversely, the bacterial protein can be made to stick. The findings have not only fundamental implications for how protein function is controlled at the physical?chemical level but can also be used to adjust protein motion in Escherichia coli at will. Twit Text FOAVip Physicochemical code for quinary protein interactions in Escherichia coli ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=28536196 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28536196 #FOAvip English Wikipedia <ref>{{Cite pmid|28536196}}</ref> Physicochemical code for quinary protein interactions in Escherichia coli #MMPMID28536196 Mu X; Choi S; Lang L; Mowray D; Dokholyan NV; Danielsson J; Oliveberg M Proc Natl Acad Sci U S A 2017[Jun]; 114 (23): E4556-63 PMID28536196show ga This study shows that the diffusive motions of proteins in live cells are by no means without control but follow simplistic physical?chemical rules that can be quantified and optimized through surface composition. Most strikingly, human proteins are observed to stick to the ?foreign? environment of bacterial cells, whereas the bacterial analogue moves around freely. Even so, the human proteins can predictably be transformed to bacterial behavior with a few structurally benign surface mutations, and, conversely, the bacterial protein can be made to stick. The findings have not only fundamental implications for how protein function is controlled at the physical?chemical level but can also be used to adjust protein motion in Escherichia coli at will. äPhysicochemical code for quinary protein interactions in Escherichia c(epmc).pdf DeepDyve Pubget Overpricing