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10.1074/jbc.R115.692715 http://scihub22266oqcxt.onion/10.1074/jbc.R115.692715 C4807256!4807256!26851275     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Biol+Chem 2016 ; 291 (13): 6689-95 Nephropedia Template TP {{tp|p=26851275|t=2016. Insights into Coupled Folding and Binding Mechanisms from Kinetic Studies* |pdf=|usr=}}{{26851275}} gab.com Text Insights into Coupled Folding and Binding Mechanisms from Kinetic Studies* JO: J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=26851275 #FOAvip Intrinsically disordered proteins (IDPs) are characterized by a lack of persistent structure. Since their identification more than a decade ago, many questions regarding their functional relevance and interaction mechanisms remain unanswered. Although most experiments have taken equilibrium and structural perspectives, fewer studies have investigated the kinetics of their interactions. Here we review and highlight the type of information that can be gained from kinetic studies. In particular, we show how kinetic studies of coupled folding and binding reactions, an important class of signaling event, are needed to determine mechanisms. Twit Text FOAVip Insights into Coupled Folding and Binding Mechanisms from Kinetic Studies* ????J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=26851275 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26851275 #FOAvip English Wikipedia <ref>{{Cite pmid|26851275}}</ref> Insights into Coupled Folding and Binding Mechanisms from Kinetic Studies* #MMPMID26851275 Shammas SL; Crabtree MD; Dahal L; Wicky BIM; Clarke J J Biol Chem 2016[Mar]; 291 (13): 6689-95 PMID26851275show ga Intrinsically disordered proteins (IDPs) are characterized by a lack of persistent structure. Since their identification more than a decade ago, many questions regarding their functional relevance and interaction mechanisms remain unanswered. Although most experiments have taken equilibrium and structural perspectives, fewer studies have investigated the kinetics of their interactions. Here we review and highlight the type of information that can be gained from kinetic studies. In particular, we show how kinetic studies of coupled folding and binding reactions, an important class of signaling event, are needed to determine mechanisms. äInsights into Coupled Folding and Binding Mechanisms from Kinetic Stud(epmc).pdf DeepDyve Pubget Overpricing