1.Researchers isolated a monomeric protein from platelets that has 2 binding sites (Aand B) for ADP; Site A's Ka is 157 μM, and Site B's Kd is 2.2 μM.1.1. A) Which binding site has higher affinity for ADP? B) Briefly justify your answer. C)For this higher affinity site, calculate the standard free energy change for ADP binding.Show your work.1.2. What concentration of ADP is required to get site A filled in 20% of the proteins?1.3. Based on this information, sketch a graph of the fraction of site B filled as a function of[ADP].

It is said that there are 2 binding sites for the ligand (the ligand here is ADP) in the protein .…

Answered: 1. Researchers isolated a monomeric…

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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2B. S. aureus hemolysin B attacks the RBC cell membrane by hydrolyzing the sphingomyelin headgroup: ОН HN .R hemolysin B cuts this bond i) Draw a plausible mechanism of hydrolysis for this lipid headgroup. Let B- and BH be general base and general acid. 00-P-O LOR2 OR, ii) Why is this damaging to the overall membrane architecture of the RBC?
1) Explain chain-folded and spherulite structures. 2) A biomedical company is planning to design a robotic arm from polymeric biomaterials based on their stress-strain curves. You as a bioengineer/researcher in this company, are requested to choose the best material from different biomaterials (A, B, C, D, E, and F) based on their mechanical properties. Express your opinion shortly on the following questions? a) Difference between A and C? b) Difference between B and D? c) Difference between F and E? d) What would be your recommendation for the robotic arm? Why? Stress (MPa) 10.0 7.5 5.0 2.5 0.0 0 D Strain (%) 10 E F 15
8) A Leu > Ala mutation at a site buried in the core of the enzyme lysozyme ends up being destabilizing. Explain why in terms of AH", AS" (for both the protein and solvent), and AG".
Consider the following properties of the protein components of a sample mixture as provided in the table below. Protein Molecular IpH Percentage of polar amino acid residues Weight (kDa) (%) АСЕ 200 7 20 CLU 25 65 DIA 100 10 40 НЕА 50 80
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.
1
You gathered your data from Lab 4, and found the following values: Total Activity of lysozyme in HEW: 14 units Total Activity of lysozyme in carb 1: 21 units Total amount of protein in HEW: 70 mg Total amount of protein in Carb 1: 15 mg Calculate the extent of purification of lysozyme in Carb 1. 150% 7 fold 70% 15 fold
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 sample of a protein is analyzed by CE using a neutral-coated capillary with a total length of 25.0 cm and a distance to the detector of 22.0 cm. Using an applied voltage of 20.0 kV, the protein was detected at a migration time of 16.2 min. The diffusion coefficient for the protein is 2.4 x 10-7 cm?/s. (a) Calculate the apparent electrophoretic mobility of the protein. (b) Calculate the expected number of theoretical plates for the analysis.
Imagine you were able to incorporate real and artificial amino acids with the following side chains into proteins. Which of these would be most likely to be found buried in the interior of the hemoglobin protein in its folded form at ~pH 7.0? a) -phenol (phenyl with -OH) b) -CH2CH3 c) -phenyl d) -CH2OH
For a binding protein to show positive cooperativity…. Choice 1 of 4:the protein must be able to adopt at least 2 different conformations each with different affinities for the ligand Choice 2 of 4:the protein must be able to bind to at least 2 different types of ligand Choice 3 of 4:the protein must bind to one molecule of ligand fast and one molecule of ligand slowly Choice 4 of 4:the Kd must be in the micromolar range
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.

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