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10.1074/jbc.R114.565515 http://scihub22266oqcxt.onion/10.1074/jbc.R114.565515 C4215204!4215204 !25210031     free     free     free Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\25210031 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       J+Biol+Chem 2014 ; 289 (44 ): 30205-30212 Nephropedia Template TP {{tp|p=25210031 |t=2014. Evolutionary aspects of enzyme dynamics |pdf=|usr=}}{{25210031 }} gab.com Text Evolutionary aspects of enzyme dynamics JO: J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=25210031 #FOAvip The role of evolutionary pressure on the chemical step catalyzed by enzymes is somewhat enigmatic, in part because chemistry is not rate-limiting for many optimized systems. Herein, we present studies that examine various aspects of the evolutionary relationship between protein dynamics and the chemical step in two paradigmatic enzyme families, dihydrofolate reductases and alcohol dehydrogenases. Molecular details of both convergent and divergent evolution are beginning to emerge. The findings suggest that protein dynamics across an entire enzyme can play a role in adaptation to differing physiological conditions. The growing tool kit of kinetics, kinetic isotope effects, molecular biology, biophysics, and bioinformatics provides means to link evolutionary changes in structure-dynamics function to the vibrational and conformational states of each protein. Twit Text FOAVip Evolutionary aspects of enzyme dynamics ????J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=25210031 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25210031 #FOAvip English Wikipedia <ref>{{Cite pmid|25210031 }}</ref> Evolutionary aspects of enzyme dynamics #MMPMID25210031 Klinman JP ; Kohen A J Biol Chem 2014[Oct]; 289 (44 ): 30205-30212 PMID25210031 show ga The role of evolutionary pressure on the chemical step catalyzed by enzymes is somewhat enigmatic, in part because chemistry is not rate-limiting for many optimized systems. Herein, we present studies that examine various aspects of the evolutionary relationship between protein dynamics and the chemical step in two paradigmatic enzyme families, dihydrofolate reductases and alcohol dehydrogenases. Molecular details of both convergent and divergent evolution are beginning to emerge. The findings suggest that protein dynamics across an entire enzyme can play a role in adaptation to differing physiological conditions. The growing tool kit of kinetics, kinetic isotope effects, molecular biology, biophysics, and bioinformatics provides means to link evolutionary changes in structure-dynamics function to the vibrational and conformational states of each protein. |*Evolution, Molecular [MESH] |Alcohol Dehydrogenase/chemistry/genetics [MESH] |Animals [MESH] |Bacterial Proteins/chemistry/genetics [MESH] |Biocatalysis [MESH] |Catalytic Domain [MESH] |Humans [MESH] |Kinetics [MESH] |Models, Chemical [MESH]Evolutionary aspects of enzyme dynamics (epmc).pdf DeepDyve Pubget Overpricing