User:Benjamin Friedel/Notebook/CHEM 471/2015/09/29: Difference between revisions
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''Figure 1: Lysozyme Fluorescence Across a-Chymotrypsin Concentrations by Wavelength'' | |||
For figure 1 below, fluorescence data for sample and blank standards A-H was corrected first by subtracted each respective blank spectra from it's sample spectra. Then the corrected absorbance at 644.5nm (the highest recorded where there should be no absorbance) was subtracted from each individual standard spectra to account for background signal. This corrected fluorescence data was plotted against the wavelength of emittance as excitation occurred at 390nm. | |||
[[Image:JNB.09.29.15 lysozymefluorescencebywavelength.png]] | |||
''Figure 2: Lysozyme AuNP Fiber Digestion by alpha-Chymotrypsin Calibration Curve'' | |||
For figure 2 below, the blank and background fluorescence curves were integrated to determine their area using the averaging method of summing rectangles composed of ([F1+F2]/2)*change in wavelength). In this case, F1 and F2 are adjacent fluorescence measurements within a standard spectra and the change in wavelength between readings was always .5nm. This integrated area was plotted agains the concentration of alpha-chymotrypsin in the sample standards. | |||
[[Image:JNB.09.29.15 fluorescencecalibrationcurve.png]] | |||
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Revision as of 05:35, 8 October 2015
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ObjectiveToday's objective is to monitor the degradation lysozyme by our protease ( alpha-chymotrypsin) over time through measuring fluorescence of lysozyme samples incubated in the with the protease over different time intervals. This experiment is controlled through also monitoring samples containing no lysozyme in the same conditions.
ProcedureDr. Hartings's protocol for the fluorescence experiment can found in his notebook. Stock Sample and Stock Blank Preparation
Fluorescence Sample and Blank Standards
Data
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