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10.1016/j.tibs.2015.09.002 http://scihub22266oqcxt.onion/10.1016/j.tibs.2015.09.002 C4630092!4630092!26481499     free     free     free       Trends+Biochem+Sci 2015 ; 40 (11): 628-47 Nephropedia Template TP {{tp|p=26481499|t=2015. Dynamics driven allostery in protein kinases |pdf=|usr=}}{{26481499}} gab.com Text Dynamics driven allostery in protein kinases JO: Trends Biochem Sci http://www.kidney.de/pget.php?&tw=1&pmid=26481499 #FOAvip Protein kinases have very dynamic structures and their functionality strongly depends on their dynamic state. Active kinases reveal a dynamic pattern with residues clustering into semirigid communities that move in µs-ms timescale. Previously detected hydrophobic spines serve as connectors between communities. Communities do not follow the traditional subdomain structure of the kinase core or its secondary structure elements. Instead they are organized around main functional units. Integration of the communities depends on the assembly of the hydrophobic spine and phosphorylation of the activation loop. Single mutations can significantly disrupt the dynamic infrastructure and thereby interfere with long distance allosteric signaling that propagates throughout the whole molecule. Dynamics is proposed to be the underlying mechanism for allosteric regulation in protein kinases. Twit Text FOAVip Dynamics driven allostery in protein kinases ????Trends Biochem Sci http://www.kidney.de/pget.php?&tw=1&pmid=26481499 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26481499 #FOAvip English Wikipedia <ref>{{Cite pmid|26481499}}</ref> Dynamics driven allostery in protein kinases #MMPMID26481499 Kornev AP; Taylor SS Trends Biochem Sci 2015[Nov]; 40 (11): 628-47 PMID26481499show ga Protein kinases have very dynamic structures and their functionality strongly depends on their dynamic state. Active kinases reveal a dynamic pattern with residues clustering into semirigid communities that move in µs-ms timescale. Previously detected hydrophobic spines serve as connectors between communities. Communities do not follow the traditional subdomain structure of the kinase core or its secondary structure elements. Instead they are organized around main functional units. Integration of the communities depends on the assembly of the hydrophobic spine and phosphorylation of the activation loop. Single mutations can significantly disrupt the dynamic infrastructure and thereby interfere with long distance allosteric signaling that propagates throughout the whole molecule. Dynamics is proposed to be the underlying mechanism for allosteric regulation in protein kinases. äDynamics driven allostery in protein kinases (epmc).pdf DeepDyve Pubget Overpricing