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10.1073/pnas.1519609113 http://scihub22266oqcxt.onion/10.1073/pnas.1519609113 C4812760!4812760!26961002     free     free     free Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Proc+Natl+Acad+Sci+U+S+A 2016 ; 113 (12): 3269-74 Nephropedia Template TP {{tp|p=26961002|t=2016. Allosteric switch regulates protein?protein binding through collective motion |pdf=|usr=}}{{26961002}} gab.com Text Allosteric switch regulates protein protein binding through collective motion JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=26961002 #FOAvip Within biological molecules, a change in shape at one site affecting a distant site is called allostery, and is a process critical for sustaining life. At the atomic level, the means of communication is often not well understood. We identify a previously unidentified way for allostery to occur through collective motion of an entire protein structure. Together with newly developed computational algorithms, we determine atomic structures representing this previously invisible allosteric motion. This allosteric network is shown to be an intrinsic property of the protein and important for enabling binding to different protein partners. The nature of this motion, along with the tools we developed to detect it, should prove invaluable for understanding living organisms and developing new therapeutics. Twit Text FOAVip Allosteric switch regulates protein protein binding through collective motion ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=26961002 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26961002 #FOAvip English Wikipedia <ref>{{Cite pmid|26961002}}</ref> Allosteric switch regulates protein?protein binding through collective motion #MMPMID26961002 Smith CA; Ban D; Pratihar S; Giller K; Paulat M; Becker S; Griesinger C; Lee D; de Groot BL Proc Natl Acad Sci U S A 2016[Mar]; 113 (12): 3269-74 PMID26961002show ga Within biological molecules, a change in shape at one site affecting a distant site is called allostery, and is a process critical for sustaining life. At the atomic level, the means of communication is often not well understood. We identify a previously unidentified way for allostery to occur through collective motion of an entire protein structure. Together with newly developed computational algorithms, we determine atomic structures representing this previously invisible allosteric motion. This allosteric network is shown to be an intrinsic property of the protein and important for enabling binding to different protein partners. The nature of this motion, along with the tools we developed to detect it, should prove invaluable for understanding living organisms and developing new therapeutics. äAllosteric switch regulates protein?protein binding through collective(epmc).pdf DeepDyve Pubget Overpricing