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

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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

  1. 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.
  2. 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.
  3. 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.
  4. 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.
  5. 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


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