Exercise 1Summarize the data below obtained from the protein experiments for determination of proteinconcentration in the form of a graph. Plot a graph containing a title and labels for both of theaxis. Three readings were taken for each protein concentration. Find the averages and standarddeviations for each reading and plot your graph using Microsoft EXCEL, complete with the errorbars. This graph representswill be used to measure the protein concentration in an unknown protein solution.calibration curve for a protein assay (next experiment) where thisConcentration of protein(Hg/mL)Absorbance, 595 nm1230.040.050.0320.120.110.1450.260.250.25100.490.490.51250.820.850.83501.281.241.25

The principle of the Bradford assay is based on the fact that the absorbance maximum for an acidic…

Answered: Summarize the data below obtained from…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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A 0.5 M phosphate buffer at pH 6.5 and a 10 mM substrate stock solution are available for preparing enzyme assays. Each assay must have a total volume of 3 mL and a final phosphate concentration of 100 mM is desired. Using the substrate concentration of 3.33 mM and 100 µL of the enzyme solution, calculate the volume of buffer, volume of substrate stock solution, and volume of water that should be place in a cuvette for the assay.
BIOCHEMISTRY Which methodologies can be used to detect the expression of a given protein? Please provide pros and cons of each mentioned approach.
The data in the table are used to create a calibration curve for the determination of RNA from its absorbance at 260 nm. Use a spreadsheet and the least-squares method to determine the slope and y-intercept of the best straight line fit to the calibration curve. Do not subtract the blank reading when creating the calibration curve. b= 0.24 Incorrect 0.00356 incorrect RNA (µg) 0.00 11.26 22.52 33.78 45.04 Absorbance at 260 nm 0.240 0.566 0.863 1.217 1.516 #g-1 Using the slope and intercept of the calibration curve, determine the quantity of RNA in a sample that gives an absorbance of t 0.828.
Which technique is used to identify an unknown protein ?
Select all that apply from the following to each transformation process : The following are White non-glowing colonies White glowing colonies Blue non-glowing colonies Blue glowing colonies None of the above The transformation are: a. LB + kanamycin plates that have been spread with the E. coli cells transformed with your ligations, what phenotype of the colonies do you expect to obtain . b. LB + kanamycin plates that have been spread with the E. coli cells transformed with water, what phenotype of the colonies do you expect to obtain. c. LB plates that have been spread with the E. coli cells transformed with your pHSG298, what phenotype of the colonies do you expect to obtain. d. LB + kanamycin plates that have been spread with the E. coli cells transformed with PHSG298, what phenotype of the colonies do you expect to obtain. e. LB plates that have been spread with the E. coli cells transformed with your ligations, what phenotype of the colonies do you expect to obtain. f. LB plates…
present briefly the principle of size exclusion chromatography. give a brief description of the use of protein assays.
Amino acid compositions can be determined by heating a protein in 6 M HCl and running the hydrolysate through an ionexchange column. If you were going to do an amino acid sequencing experiment, why would you want to get an amino acid composition first?
IN A BIURET ASSAY TWO PROTEIN SOLUTION CONTAINING 150MG/ML AND 180MG/ML SHOWS THE SIMILAR ABSORBANCE. IS IT POSSIBLE?
In DNA purification, explain how the chromosomal DNA is separated from the plasmid DNA? Be sure to mention the specific buffer components that facilitate this process.
topic: Preparation of a Calibration CurveStandard Bovine Serum Albumin (BSA) solution Why is BSA used as a standard for protein content determination? Can other proteins be usedinstead?
Protein analysis by gel electrophoresis a). Using the gel image provided to calculate the electrophoretic relative mobility as a ratio of the distance of protein migration to the distance of the tracking dye migration (See Appendix B). If your dye front is not visible, measure the mobility relative to the bottom edge of the resolving gel. Include a labeled print-out of your gel image with your report. b). Plot log MW of the protein markers and commercial myoglobin vs. mobility. Determine the molecular weight of myoglobin obtained after the final purification step (Sample E) from the equation of the line. Submit a copy of your graph along with the gel image. c). Compare your sample E and commercial myoglobin with the ladder. Summary your results. order of sample (left to right) is : A B C D blank E blank Commercial Myoglobin Molecular Ladder
You have a 20 mg/ml of Ethidium bromide stock solution. You need to a final concentration of 2ug/ml into a Agarose solution to visualize DNA. What is the dilution factor? Give typing answer with explanation and conclusion

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