You will have to dilute your inital Lysozyme stock in order to pipet volumeslarger than 10 uL for the Bradford assay. Calculate a dilution of the 10mg/mL Lysozyme standard needed to create ensure an appropriate finalprotein range for the Bradford assay - what concentration will your Lysozymestandard be at for the Bradford assay?

Step 1:For the Bradford assay, the typical concentration range of protein you want to target is…

Answered: You will have to dilute your inital…

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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why are lysozyme and ovoalbumin the recommended standards used in the Bradford protein assay and why would they be preferred over BSA being this widely used but not recommended? Justify the answer
At higher amounts of protein, the Bradford assay is not linear. Consider the plot to the right: what is the maximum amount of protein a sample could contain and still fall within a standard curve? Briefly explain your reasoning.
Using the SDS-PAGE and the calibration curve given, calculate the size of the lysozyme and ovalbumin bands from this lysozyme purification. Lysozyme is the bottom band in the samples, ovalbumin is the most intense band in the first three samples, and the first and last lanes are molecular mass standards.
A number of techniques can separate proteins on the basis of their differences in mass. Describe the use of two of these techniques, centrifugation and gel electrophoresis. The blood proteins transferrin (MW 76 kDa) and lysozyme (MW 15 kDa) can be separated by rate zonal centrifugation or SDS-polyacrylamide gel electrophoresis. Which of the two proteins will sediment faster during centrifugation? Which will migrate faster during electrophoresis?
If 1ml of an unknown sample of protein is diluted to 10ml, and a 0.5ml portion of the diluted sample is found to contain 50ug of protein when assayed for protein using the lowry method. If you mix two unknown samples and repeat the lowry assay, is the absorbance equivalent to the sum of the two individual unknown samples that is used?
IN A BIURET ASSAY TWO PROTEIN SOLUTION CONTAINING 150MG/ML AND 180MG/ML SHOWS THE SIMILAR ABSORBANCE. IS IT POSSIBLE?
Increasing the saturation of the ammonium sulfate is a prerequisite in isolating a target protein that is rich in Cys and Tyr residues. Which of the following techniques should be considered in accurately quantifying the isolated protein?I. Running the isolated protein in a dialysis or GFC set up.II. Using Biuret or BCA assay as the colorimetric quantitation method.III. Using Bradford or Lowry assay as the colorimetric quantitation method.A. I onlyB. II onlyC. I and IIID. I, II and IIIBradford Assay is most suitable to use when the extraction buffer is below the target protein’s pI. This is so because the protein would be morea. Positively charged allowing the CBB G-250 dye to bind via its sulfonate groups.b. Negatively charged allowing the CBB G-250 dye to bind via its sulfonate groups.c. Neutrally charged allowing the CBB G-250 dye to bind via its sulfonate groups.d. Zwitterionic allowing the CBB G-250 dye to bind via its sulfonate groups.
For the following sequence, what is the approximate annealing temperature? 5'-AGCTACGATCAGGTCA-3'
Since myoglobin is red and it may interfere with the absorbance of Bradford Protein Assay at OD595nm, how can you determine whether the effect of the interference is significant?
Sketch the appearance after visualization of a protein mixture containing the seven proteins (fibrinogen, y-globulin, collagen, ovalbumin, myoglobin, hemoglobin, insulin) when subjected to two-dimensional (2D) gel electrophoresis.
After calculating the extinction coefficient for lysozyme above, you convert it into ml mg cm1 units. (You need not do the calculation, just suppose you did). To calculate the protein concentration in your column fractions (W1-3, E1-2), would your calculated extinction coefficient be a better choice than 1.5 mL mg 1 cm1 value listed in the theory section of your pre-lab? Why or why not? (Choose the best response) Yes, because we expect all of the column fractions to be mainly lysozyme. No, because most, if not all, the column fractions are mixtures of 2 or more proteins. Trick question, we should use the values calculated by EXPASY for lysozyme. Yes, because my calculated value is more accurate than values from the literature. ONo, because lysozyme is still stuck to the column and shouldnot be in any of our column fractions.
Calculate the melting temperature (TM) for the GFP primer CATGGTCCTGCTGGAGTTCGTG. Answer to 2 significant figures. .....

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