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10.1098/rsfs.2013.0077 http://scihub22266oqcxt.onion/10.1098/rsfs.2013.0077 C3996589!3996589 !24904740     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=24904740 &cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\24904740 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Interface+Focus 2014 ; 4 (3 ): 20130077 Nephropedia Template TP {{tp|p=24904740 |t=2014. A queueing approach to multi-site enzyme kinetics |pdf=|usr=}}{{24904740 }} gab.com Text A queueing approach to multi-site enzyme kinetics JO: Interface Focus http://www.kidney.de/pget.php?&tw=1&pmid=24904740 #FOAvip Multi-site enzymes, defined as where multiple substrate molecules can bind simultaneously to the same enzyme molecule, play a key role in a number of biological networks, with the Escherichia coli protease ClpXP a well-studied example. These enzymes can form a low latency 'waiting line' of substrate to the enzyme's catalytic core, such that the enzyme molecule can continue to collect substrate even when the catalytic core is occupied. To understand multi-site enzyme kinetics, we study a discrete stochastic model that includes a single catalytic core fed by a fixed number of substrate binding sites. A natural queueing systems analogy is found to provide substantial insight into the dynamics of the model. From this, we derive exact results for the probability distribution of the enzyme configuration and for the distribution of substrate departure times in the case of identical but distinguishable classes of substrate molecules. Comments are also provided for the case when different classes of substrate molecules are not processed identically. Twit Text FOAVip A queueing approach to multi-site enzyme kinetics ????Interface Focus http://www.kidney.de/pget.php?&tw=1&pmid=24904740 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=24904740 #FOAvip English Wikipedia <ref>{{Cite pmid|24904740 }}</ref> A queueing approach to multi-site enzyme kinetics #MMPMID24904740 Hochendoner P ; Ogle C ; Mather WH Interface Focus 2014[Jun]; 4 (3 ): 20130077 PMID24904740 show ga Multi-site enzymes, defined as where multiple substrate molecules can bind simultaneously to the same enzyme molecule, play a key role in a number of biological networks, with the Escherichia coli protease ClpXP a well-studied example. These enzymes can form a low latency 'waiting line' of substrate to the enzyme's catalytic core, such that the enzyme molecule can continue to collect substrate even when the catalytic core is occupied. To understand multi-site enzyme kinetics, we study a discrete stochastic model that includes a single catalytic core fed by a fixed number of substrate binding sites. A natural queueing systems analogy is found to provide substantial insight into the dynamics of the model. From this, we derive exact results for the probability distribution of the enzyme configuration and for the distribution of substrate departure times in the case of identical but distinguishable classes of substrate molecules. Comments are also provided for the case when different classes of substrate molecules are not processed identically. äA queueing approach to multi-site enzyme kinetics (epmc).pdf DeepDyve Pubget Overpricing