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Fig. 1 | BMC Bioinformatics

Fig. 1

From: ICEKAT: an interactive online tool for calculating initial rates from continuous enzyme kinetic traces

Fig. 1

Interactive continuous enzyme kinetic analysis tool. a Click "Upload Local File" to begin analysis of user CSV formatted data. b Use dropdown menus to select between Michaelis-Menten, IC50/EC50, and high-throughput screening (HTS) modes, choose y-axis sample, and select a blank sample for subtraction. Use the boxes to "Enter Transform Equation" to transform measured signal into substrate concentration and to enter a time delay between mixing and first read (used in "Logarithmic Fit" mode only). Advanced settings for pIC50/EC50 analysis to transform the input concentration values from a linear to a log scale for analysis and plotting, fix the bottom and/or top of the fitted curve to a particular value, and/or fix the Hill slope of the fitted curve to a particular value (typically 1). c Click buttons to select routine for fitting the kinetic traces. The default is to maximize the slope magnitude. d Representative continuous enzyme kinetic trace (grey) with initial rate fit (red) corresponding to the selected y-axis sample. e Plot of a Michaelis-Menten fit to the calculated initial rates. f Data table containing initial rate values and model fit values with errors propagated from the initial rate fits. Use the "Download Table to CSV" or "Copy Table to Clipboard" buttons to export initial rate values from the data table. g Plot of the residuals from the kinetic trace initial rate fit in d. The "Enter Start Time" and "Enter End Time" boxes and fine tune slider allow the user to optimize the x-axis time domain of the fit to obtain a random residual distribution

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