User:Tamra L. Fisher/Notebook/Experimental Biological Chem/2011/10/05

AU Biomaterials Design Lab

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Objective Take fluorescent spectra of the maltose-binding protein (MBP). Description The calculated concentration of the MBP protein on 9/13/11 was 10.714μM First, the 10.714μM MBP was diluted by mixing 1397μL of it with 1603μL of 50mM Tris buffer, pH 7.55. This gave a final concentration of 4.989μM. The intensities of this was taken from 310nm-500nm when excited at 290nm. Then, 300μL of the 4.989μM MBP was diluted with 2700μL of the same Tris buffer for a final concentration of 0.4989μM. The intensities of this was taken from 310nm-500nm when excited at 290nm. Then, 300μL of the 0.4989μM MBP was diluted with 2700μL of the same Tris buffer for a final concentration of 49.89nM. The intensities of this was taken from 310nm-500nm when excited at 290nm. Then, 300μL of the 49.89nM MBP was diluted with 2700μL of the same Tris buffer for a final concentration of 4.989nM. The intensities of this was taken from 310nm-500nm when excited at 290nm. Then, 300μL of the 4.989nM MBP was diluted with 2700μL of the same Tris buffer for a final concentration of 0.4989nM. The intensities of this was taken from 310nm-500nm when excited at 290nm. Data The intensities of the different concentrations of MBP were corrected with the intensities of the Tris buffer. The intensities were plotted against the wavelengths (note: some of the MBP concentrations were too concentrated for a correct intensity reading): The intensities divided by the concentrations of MBP vs. the wavelengths was also plotted: Notes