Use my Search Websuite to scan PubMed, PMCentral, Journal Hosts and Journal Archives, FullText. Kick-your-searchterm to multiple Engines kick-your-query now !>

A dictionary by aggregated review articles of nephrology, medicine and the life sciences Your one-stop-run pathway from word to the immediate pdf of peer-reviewed on-topic knowledge.

10.1038/s41467-018-03597-y http://scihub22266oqcxt.onion/10.1038/s41467-018-03597-y C5862990!5862990!29563521     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       Nat+Commun 2018 ; 9 (ä): ä Nephropedia Template TP {{tp|p=29563521|t=2018. Dynamical origins of heat capacity changes in enzyme-catalysed reactions |pdf=|usr=}}{{29563521}} gab.com Text Dynamical origins of heat capacity changes in enzyme-catalysed reactions JO: Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=29563521 #FOAvip Heat capacity changes are emerging as essential for explaining the temperature dependence of enzyme-catalysed reaction rates. This has important implications for enzyme kinetics, thermoadaptation and evolution, but the physical basis of these heat capacity changes is unknown. Here we show by a combination of experiment and simulation, for two quite distinct enzymes (dimeric ketosteroid isomerase and monomeric alpha-glucosidase), that the activation heat capacity change for the catalysed reaction can be predicted through atomistic molecular dynamics simulations. The simulations reveal subtle and surprising underlying dynamical changes: tightening of loops around the active site is observed, along with changes in energetic fluctuations across the whole enzyme including important contributions from oligomeric neighbours and domains distal to the active site. This has general implications for understanding enzyme catalysis and demonstrating a direct connection between functionally important microscopic dynamics and macroscopically measurable quantities. Twit Text FOAVip Dynamical origins of heat capacity changes in enzyme-catalysed reactions ????Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=29563521 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29563521 #FOAvip English Wikipedia <ref>{{Cite pmid|29563521}}</ref> Dynamical origins of heat capacity changes in enzyme-catalysed reactions #MMPMID29563521 van der Kamp MW; Prentice EJ; Kraakman KL; Connolly M; Mulholland AJ; Arcus VL Nat Commun 2018[]; 9 (ä): ä PMID29563521show ga Heat capacity changes are emerging as essential for explaining the temperature dependence of enzyme-catalysed reaction rates. This has important implications for enzyme kinetics, thermoadaptation and evolution, but the physical basis of these heat capacity changes is unknown. Here we show by a combination of experiment and simulation, for two quite distinct enzymes (dimeric ketosteroid isomerase and monomeric alpha-glucosidase), that the activation heat capacity change for the catalysed reaction can be predicted through atomistic molecular dynamics simulations. The simulations reveal subtle and surprising underlying dynamical changes: tightening of loops around the active site is observed, along with changes in energetic fluctuations across the whole enzyme including important contributions from oligomeric neighbours and domains distal to the active site. This has general implications for understanding enzyme catalysis and demonstrating a direct connection between functionally important microscopic dynamics and macroscopically measurable quantities. äDynamical origins of heat capacity changes in enzyme-catalysed reactio(epmc).pdf DeepDyve Pubget Overpricing