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6 results for “Enzyme Kinetics”
Computational models from: Allele-specific activation, enzyme kinetics, and inhibitor sensitivities of EGFR exon 19 deletion mutations in lung cancer
<p>Computational models, compressed molecular dynamics (MD) simulation trajectories, and sample input files for "Allele-specific activation, enzyme kinetics, and inhibitor sensitivities of EGFR exon 19 deletion mutations in lung cancer". An early version of this manuscript is available as a preprint here: https://www.biorxiv.org/content/10.1101/2022.03.16.484661v1</p>
The measurement of true initial rates is not always absolutely necessary to estimate enzyme kinetic parameters
<p>Dataset of Excel files used for the publication.</p>
MD trajectories for "Kinetic barrier to enzyme inhibition is manipulated by dynamical local interactions in E. coli DHFR"
<p>Dihydrofolate reductase (DHFR) is an important drug target and a highly studied model<br> protein for understanding enzyme dynamics. DHFR’s crucial role in folate synthesis renders it<br> an ideal candidate to understand protein function and protein evolution mechanisms. In this<br> study, to understand how a newly proposed DHFR inhibitor, 4’-deoxy methyl trimethoprim<br> (4’-DTMP), alters evolutionary trajectories, we studied interactions that lead to its superior<br> performance over trimethoprim (TMP). To elucidate the inhibition mechanism of 4’-DTMP,<br> we first confirmed, both computationally and experimentally, that the relative binding free<br> energy cost for the mutation of TMP and 4’-DTMP are the same, pointing to the origin of the<br> characteristic differences to be kinetic rather than thermodynamic. We then employed an<br> interaction-based analysis by focusing first on the active site, then on the whole enzyme. We<br> confirmed that the polar modification in 4’-DTMP induces additional local interactions with<br> the enzyme, particularly the M20 loop. These changes are propagated to the whole enzyme as<br> shifts in the hydrogen bond networks. To shed light on the allosteric interactions, we support<br> our analysis with network-based community analysis and show that segmentation of the loop<br> domain of the inhibitor-bound DHFR must be avoided by a successful inhibitor.</p>
Dataset for manuscript "Turnover number predictions for kinetically uncharacterized enzymes using machine and deep learning"
<p>Dataset for the github repository containing the code for the manuscript "Turnover number predictions for kinetically uncharacterized enzymes using machine and deep learning".</p>
Soil microbial biomass and enzyme kinetics for the assessment of temporal diversification in agroecosystems
Open the record for dataset details and reuse information.
Kinetic Study Of Supplementation With The Enzyme Diamine Oxidase In Patients With Histamine Intolerance
ClinicalTrials.gov study NCT07006558. IPD Sharing: YES. Countries: 1. Publications: 0.
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