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10.1038/srep27808 http://scihub22266oqcxt.onion/10.1038/srep27808 C4906287!4906287 !27298067     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=27298067 &cmd=llinks): Failed to open stream: HTTP request failed! 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Energy Landscape Topography Reveals the Underlying Link Between Binding Specificity and Activity of Enzymes |pdf=|usr=}}{{27298067 }} gab.com Text Energy Landscape Topography Reveals the Underlying Link Between Binding Specificity and Activity of Enzymes JO: Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=27298067 #FOAvip Enzyme activity (often quantified by kcat/Km) is the main function of enzyme when it is active against the specific substrate. Higher or lower activities are highly desired for the design of novel enzyme and drug resistance. However, it is difficult to measure the activities of all possible variants and find the "hot-spot" within the limit of experimental time. In this study, we explore the underlying energy landscape of enzyme-substrate interactions and introduce the intrinsic specificity ratio (ISR), which reflects the landscape topography. By studying two concrete systems, we uncover the statistical correlation between the intrinsic specificity and the enzyme activity kcat/Km. This physics-based concept and method show that the energy landscape topography is valuable for understanding the relationship between enzyme specificity and activity. In addition, it can reveal the underlying mechanism of enzyme-substrate actions and has potential applications on enzyme design. Twit Text FOAVip Energy Landscape Topography Reveals the Underlying Link Between Binding Specificity and Activity of Enzymes ????Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=27298067 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27298067 #FOAvip English Wikipedia <ref>{{Cite pmid|27298067 }}</ref> Energy Landscape Topography Reveals the Underlying Link Between Binding Specificity and Activity of Enzymes #MMPMID27298067 Chu WT ; Wang J Sci Rep 2016[Jun]; 6 (ä): 27808 PMID27298067 show ga Enzyme activity (often quantified by kcat/Km) is the main function of enzyme when it is active against the specific substrate. Higher or lower activities are highly desired for the design of novel enzyme and drug resistance. However, it is difficult to measure the activities of all possible variants and find the "hot-spot" within the limit of experimental time. In this study, we explore the underlying energy landscape of enzyme-substrate interactions and introduce the intrinsic specificity ratio (ISR), which reflects the landscape topography. By studying two concrete systems, we uncover the statistical correlation between the intrinsic specificity and the enzyme activity kcat/Km. This physics-based concept and method show that the energy landscape topography is valuable for understanding the relationship between enzyme specificity and activity. In addition, it can reveal the underlying mechanism of enzyme-substrate actions and has potential applications on enzyme design. |*Catalysis [MESH] |*Protein Binding [MESH] |*Thermodynamics [MESH] |Binding Sites [MESH] |Crystallography, X-Ray [MESH] |Endorphins/chemistry [MESH] |Enzyme Activation [MESH] |Humans [MESH] |Kinetics [MESH] |Peptide Fragments/chemistry [MESH] |Phosphoprotein Phosphatases/chemistry [MESH]Energy Landscape Topography Reveals the Underlying Link Between Bindin(epmc).pdf DeepDyve Pubget Overpricing