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10.1146/annurev-biochem-061809-100742 http://scihub22266oqcxt.onion/10.1146/annurev-biochem-061809-100742 C5502542!5502542!21675920     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 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Annu+Rev+Biochem 2011 ; 80 (ä): 703-32 Nephropedia Template TP {{tp|p=21675920|t=2011. Enzymatic Transition States, Transition-State Analogs, Dynamics, Thermodynamics, and Lifetimes |pdf=|usr=}}{{21675920}} gab.com Text Enzymatic Transition States, Transition-State Analogs, Dynamics, Thermodynamics, and Lifetimes JO: Annu Rev Biochem http://www.kidney.de/pget.php?&tw=1&pmid=21675920 #FOAvip Experimental analysis of enzymatic transition-state structures uses kinetic isotope effects (KIEs) to report on bonding and geometry differences between reactants and the transition state. Computational correlation of experimental values with chemical models permits three-dimensional geometric and electrostatic assignment of transition states formed at enzymatic catalytic sites. The combination of experimental and computational access to transition-state information permits (a) the design of transition-state analogs as powerful enzymatic inhibitors, (b) exploration of protein features linked to transition-state structure, (c) analysis of ensemble atomic motions involved in achieving the transition state, (d) transition-state lifetimes, and (e) separation of ground-state (Michaelis complexes) from transition-state effects. Transition-state analogs with picomolar dissociation constants have been achieved for several enzymatic targets. Transition states of closely related isozymes indicate that the protein?s dynamic architecture is linked to transition-state structure. Fast dynamic motions in catalytic sites are linked to transition-state generation. Enzymatic transition states have lifetimes of femtoseconds, the lifetime of bond vibrations. Binding isotope effects (BIEs) reveal relative reactant and transition-state analog binding distortion for comparison with actual transition states. Twit Text FOAVip Enzymatic Transition States, Transition-State Analogs, Dynamics, Thermodynamics, and Lifetimes ????Annu Rev Biochem http://www.kidney.de/pget.php?&tw=1&pmid=21675920 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=21675920 #FOAvip English Wikipedia <ref>{{Cite pmid|21675920}}</ref> Enzymatic Transition States, Transition-State Analogs, Dynamics, Thermodynamics, and Lifetimes #MMPMID21675920 Schramm VL Annu Rev Biochem 2011[]; 80 (ä): 703-32 PMID21675920show ga Experimental analysis of enzymatic transition-state structures uses kinetic isotope effects (KIEs) to report on bonding and geometry differences between reactants and the transition state. Computational correlation of experimental values with chemical models permits three-dimensional geometric and electrostatic assignment of transition states formed at enzymatic catalytic sites. The combination of experimental and computational access to transition-state information permits (a) the design of transition-state analogs as powerful enzymatic inhibitors, (b) exploration of protein features linked to transition-state structure, (c) analysis of ensemble atomic motions involved in achieving the transition state, (d) transition-state lifetimes, and (e) separation of ground-state (Michaelis complexes) from transition-state effects. Transition-state analogs with picomolar dissociation constants have been achieved for several enzymatic targets. Transition states of closely related isozymes indicate that the protein?s dynamic architecture is linked to transition-state structure. Fast dynamic motions in catalytic sites are linked to transition-state generation. Enzymatic transition states have lifetimes of femtoseconds, the lifetime of bond vibrations. Binding isotope effects (BIEs) reveal relative reactant and transition-state analog binding distortion for comparison with actual transition states. äEnzymatic Transition States, Transition-State Analogs, Dynamics, Therm(epmc).pdf DeepDyve Pubget Overpricing