Consider five proteins with the properties shown in the following table. Answer the questions belowabout these proteins and justify your answers.Protein Subunit mass (Da) | Native mass (Da)10,00040,000120,000A15,000C20,00020,00025,00075,000E30,00060,000a) Which protein would migrate the slowest in an SDS-PAGE? Justify your results.b) Which protein would migrate the fast in a Native-PAGE? Justify your results.

Protein is an organic nitrogenous macromolecule that is essential for the health of humans. In the…

Answered: Consider five proteins with the…

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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You have a soluble protein that is highly flexible and is only 23 kDa in size. What is the most suitable technique (X-ray crystallography, NMR, cryo-EM) for structure determination of this protein? Explain your reasoning.
You perform electrophoresis of 3 proteins, Hemoglobin (pl: 6.8), DNA Polymerase (pl: 5.2) and Porcine pepsin (pl: 1.0) in a Tris-Glycine buffer (pH 5.2). (pl = Isoelectric point). Select which of the following is true. O All proteins will migrate at the same rate O All proteins will migrate at the same direction Porcine pepsin will migrate toward the electrode Porcine pepsin will not migrate and stay in the well
Four proteins Cytochrome C (pI=10.2) Myoglobin (pI=7.2), Hemoglobin (pI = 6.8) and Serum Albumin (pI= 4.8) were used in our gel electrophoresis lab exercise. What is the molecular basis for the differences in the electrophoretic mobilities of the four proteins analyzed in this exercises? size shape charge all of them
6. Consider the following proteins to answer the questions below: Protein Size (kDa) pl ε at 280 nm 10 4 7000 50 4 14000 10 8 3000 50 8 50000 A B C C Red Colored? Yes No No No b. Describe a two-step purification procedure that could be used to purify/isolate protein A from the other proteins. In your response, describe the type of chromatography used, the pH of buffer needed, and a labeled chromatogram (include absorbances at both 280 and 400 nm). Make sure you note which "fraction/sample" is needed from the first step to proceed/use for the second step. Use another page if necessary.
Fill the table given the info below. Please thank you. Protein at 1 mg/mL which is also 1g/L. Use the DNA sequence below to export to ExPASy Translate & ProtParam. (I tried doing so and I calculated a Molarity of 16.51uM which came from the 60,567.28Da from ExPASy). Using the molarity then use it to fill out the table.…
The elution of a protein with an isoelectric point of 7.5, is mostly likely to be affected by a change in pH from 7.4 to 6.9 in which type of protein separation technique? a.) size exclusion chromatography b.) SDS-acrylamide gel electrophoresis c.) affinity chromatography d.) ion exchange chromatography
A recent genome sequencing project for the bacterium Burkholderia mallei has identified a new protein with high similarity to the lysylphosphatidylglycerol flippase enzyme. A short section of the new protein sequence is shown below. TVEVNAPGDVQKALSELQQINDGRLDIRI (a) Are any reverse turns likely to be present? Explain your answer. (b) Are any beta-strands likely to be present? Explain your answer. (c) Are any alpha helices likely to be present? Explain your answer. (d) Is any supersecondary structure likely to be present? Explain your answer. (e) Identify two residues that are likely to be buried in the core of the folded protein. Explain your answer. (f) Identify two residues that are likely to be hydrogen bonded to each other. Explain your answer.
Membrane-spanning proteins are notoriously difficult to characterize by x-ray crystallography. Hollonut of VISA Toplon a. Explain how the information in the diagrams below can be used in the detection of membrane- spanning proteins consisting of alpha helices, given that the lipid portion of a typical bilayer is approximately 30 Å thick. Amino terminus 5.4 A (3.6 residues) b. Identify and briefly describe how the features of a transmembrane protein composed of ß-sheets differ from that above.
1.0.1 mL of a protein solution of concentration of 11 mg/mL was diluted to a total volume of 4.0 mL with water (i.e. 0.1 mL of the solution was added to 3.9 mL of water). 2 mL of this solution was then mixed with 18 mL of water. What is the concentration of the diluted protein solution? Space to show your workings:
A solution containing two globular proteins each with a single subunit (one is "large" with a radius of 47 Å and the other is "small" with a radius of 16 A) is applied to a gel-filtration (i.e. size-exclusion) column. What is the most likely outcome? O a The outcome will depend on which protein has the most negative surface charge. O b. The small protein elutes before the large protein. O C. The large protein elutes before the small protein. O d. Both proteins elute together. O e. The outcome will depend on the pH of the solution.
A protein was purified and then analyzed on a size exclusion column. Its MW was determined to be 50,000 Dalton. The SDS-PAGE gel shows two bands, corresponding to molecular weights of 10,000 and 15,000 Dalton. Describe the native conformation of this protein in terms of the number of subunits present and their molecular weight.
Two proteins, A and B, bind to the same ligand, L, with the binding curvesshown below. What is the dissociation constant, Kd , for each protein? Which protein (A or B) has a greater affinity for ligand L?

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