Multi panel figure legend PDF

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Summary

Example of how a multipanel figure legend should look for cell bio lab with Dr. DeWitt. Complete with figure legend examples and necessary graphing aspects....

Description

0.7

Rate (M/s)

0.6

f(x) = 0.3 ln(x) + 0.07 R² = 0.98

0.5 0.4 0.3 0.2 0.1 0

0

1

2

3

4

5

6

7

50

60

70

Conc

PNPP Concentraton (mM)

5 0

0

10

20

30

40

Time (s)

Figure 1. Michaelis-Menten and Lineweaver Burk Vmax and Km estimations from enzyme assays of the alkaline phosphatase and PNPP reaction. The experimental optimal amount of alkaline phosphatase was determined to be 11 uL with a ΔA per minute of .495. 11 uL of enzyme was used to test each assay of PNPP concentration (.004-.400 mM) run at 410 nm, as seen in 1a. The absorbance values of the assays were converted to concentrations based on the line of best fit from the standard curve of PNP (10-50 µM). The slope from each enzyme assay was used to create the 1b. MichaelisMenten plot which showed an approximate Km value of 0.054 mM and a reaction Vmax of 0.616 µM/s based on the asymptote of the graph. When the reciprocal values from 1b. were used to create the Lineweaver-Burk 1c., the Km was negative reciprocal of the x-intercept and had a value of 0.049mM while the Vmax of the reaction was the reciprocal of the y-intercept and was calculated to be 0.616 µM/s Figure 1. Michaelis-Menten and Lineweaver Burk Vmax and Km estimations from enzyme assays of the alkaline phosphatase and PNPP reaction. The experimental optimal amount of alkaline phosphatase was determined to be 11 uL with a delta A per minute of .495. 11 ul of enzyme was used to test each assay of PNPP concentration (.004-.400 mM) run at 410 nm, as seen in 1a. The absorbance values of the assays were converted to concentrations based on the line of best fit from the standard curve of PNP (10-50 µM). The slope from each enzyme assay was used to create the 1b. Michaelis-Menten plot which showed an approximate Km value of 0.054 mM and a reaction Vmax of 0.616 µM/s based on the asymptote of the graph. When the reciprocal values from 1b. were used to create the Lineweaver-Burk 1c., the Km was negative inverse of the x-intercept and had a value of 0.049mM while the Vmax of the reaction was the inverse of the y-intercept and was calculated to be 0.616 µM/s...