User:Nicole Bonan/Notebook/Chem 571 Lab Notebook/2015/09/30: Difference between revisions
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===Fluorescence=== | ===Fluorescence=== | ||
<center>Figure 1: Fluorescence of Lysozyme in Varying Concentrations of alpha-Chymotrypsin (nM) as a Function of the Wavelength of Incident Light (nm)</center> | <center><b>Figure 1: Fluorescence of Lysozyme in Varying Concentrations of alpha-Chymotrypsin (nM) as a Function of the Wavelength of Incident Light (nm)</b></center> | ||
[[Image:20150930 fluorescence curves bonan.png|thumb|center|700px]] | [[Image:20150930 fluorescence curves bonan.png|thumb|center|700px]] | ||
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The above figure shows the fluorescence of lysozyme in samples of varying concentrations of alpha-chymotrypsin as a function of the wavelength of incident light. The fluorescence of each sample was corrected for the blanks by subtracting the fluorescence of the blank from the fluorescence of the sample for every wavelength measured. Each curve on the graph represents a different concentration of alpha-chymotrypsin. | The above figure shows the fluorescence of lysozyme in samples of varying concentrations of alpha-chymotrypsin as a function of the wavelength of incident light. The fluorescence of each sample was corrected for the blanks by subtracting the fluorescence of the blank from the fluorescence of the sample for every wavelength measured. Each curve on the graph represents a different concentration of alpha-chymotrypsin. | ||
<center>Figure 2: Fluorescence Intensity of Lysozyme as a Function of the Concentration of alpha-Chymotrypsin</center> | <center><b>Figure 2: Fluorescence Intensity of Lysozyme as a Function of the Concentration of alpha-Chymotrypsin</b></center> | ||
[[Image:20150930 bonan fluorescence intensity.png|thumb|center|700px]] | [[Image:20150930 bonan fluorescence intensity.png|thumb|center|700px]] |
Revision as of 14:30, 7 October 2015
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ObjectiveThe purpose of today's lab work is to:
ProtocolDr. Hartings's protocol for today is here. We are following his protocols for fluorescence and for the Bradford Assay. Fluorescence Analysis of Protease DegradationYesterday, we measured the fluorescence of all of our samples of alpha-chymotrypsin + lysozyme. Today, we finished the fluorescence measurements for the alpha-chymotrypsin blanks as follows:
Brasford Analysis of Protease Degradation
Data and AnalysisFluorescenceThe above figure shows the fluorescence of lysozyme in samples of varying concentrations of alpha-chymotrypsin as a function of the wavelength of incident light. The fluorescence of each sample was corrected for the blanks by subtracting the fluorescence of the blank from the fluorescence of the sample for every wavelength measured. Each curve on the graph represents a different concentration of alpha-chymotrypsin. The above image shows the fluorescence intensity of lysozyme as a function of the concentration of alpha-chymotrypsin that it is reacted with. Bradford AssayThe figure above shows the absorbance of the blank as a function of the wavelength of incident light. The blank is the same blank that was made and measured in the protocol from September 23. This blank consisted of the Bradford Assay Reagent, Bradford Assay Buffer, and 50mM Tris + 50mM NaCl buffer. There was no protease, protein, or AuNP in this blank. The figure above shows the absorbance of the alpha-chymotrypsin blanks as a function of the wavelength of incident light. Each colored curve represents a blank that was incubated for a specific amount of time, as indicated in the legend.
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