Please help me solve 3 and explain the process in order to understand. 3. Consider Anfinsen's classical protein folding experiment.SHG=ANative(100% active)ĞNative1. Reduce2.8 M urea1. Reduce2.8 M ureaSHSHHSDenatured(inactive)SHSHSHSHSHDenatured1. Remove urea2. Oxidize1. Oxidize2. Remove ureaABa. What do you expect to be the results of Experiment A versus Experiment B above. Explain.b. In Anfinsen's experiment, the Ribonuclease protein will fold correctly even if kept in a reducingenvironment (all disulfide bonds broken). What are the main driving forces that lead to properfolding?c. What is the main force that opposes folding?

Conclusion: Anfinsen's experiment demonstrated that the amino acid sequence of a protein…

Answered: 3. Consider Anfinsen's classical…

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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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.…
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.
In the protein denaturation experiment, which of the following can be a consequence of the air bubbles in the viscometry run for an aqueous solution of protein with a denaturant?a. Increased t0b. Decreased t0c. Increased nspd. Decreased nspAll of the statements about protein denaturation are true EXCEPT:a. The viscosity of linear proteins is greater than that of the globular proteins.b. Only the BME can disrupt a covalent bond while the other denaturants can just disrupt non-covalent bonds.c. Protein renaturation is possible but in some cases protein denaturation proceeds to protein degradation. d. Protein denaturation generally disrupts tertiary or quaternary structures only
5. The proteins listed below are separated by (1) isoelectric focusing (IEF) followed by (2) sodium dodecyl sulfate- polyacrylamide gel electrophoresis (SDS-PAGE). A single sample of the protein mixture is placed at the top center of the gel to begin step 1. ID 1 2 3 4 5 6 7 8 Protein Collagen y-Globulin Insulin Fibronectin Lysozyme Pepsin Serum Albumin Myoglobin Molecular Weight 300,000 150,000 5,700 220,000 14,300 34,500 66,500 16,700 Conc pl 0.5 mg/L 4.7 1 mg/L 7.2 12 mg/L 5.3 5.8 11.0 5 mg/L 2 mg/L 10 mg/L - added prior to running IEF? left out of the process entirely? 4 mg/L 2 mg/L 1.0 4.9 7.1 A. Which of these proteins would electrophoresis NOT separate effectively? B. Which of these proteins would isoelectric focusing NOT separate effectively? Type fibrous a-helices globular protein globular protein fibrous protein enzyme digestive enzyme blood protein muscle protein C. Show the expected results after each step, by drawing qualitative diagrams similar to those shown in the class…
6a. Using your 5 mg/mL stock solution, you wish to make 100µL of the correct concentration of protein to load. How do you make this working solution? (Yes- you would want this to be in 1x sample buffer, but that makes this question more complicated. So for this question just make the protein in water.) Volume of 10mg/ml Final Volume ! 1 100μL of protein 6b. This is a 1: A N Body* @ 2 W S dilution. #3 X E D $ 4 A C R F B I % 5 T V MacBook Pro U וכ H E U 8 N J ( 0
8L.Part I
Exhibit 8A 3. Refer to Exhibit 8A. The most likely method to get protein 3 into a solution is by using? O a. 6M HCI O b. NAOH C. SDS o d. beta merchaptoethanol e. centrifugation
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
2. During SDS PAGE, Tighnari loaded the purified protein extract from redcrest and padisarah, another sample that he is working with for his dissertation. Note that the isolated proteins from padisarah have molecular weights similar to that of the proteins isolated from redcrest. The results of the SDS-PAGE are shown in Figure D.2. SDS-PAGE w/o ß-mercaptoethanol LANE 1 B D LANE 2 PHILGAR SDS-PAGE w/ p-mercaptoethanol LANE 1 !!! LANE 2 Figure D.2. Electrophoretogram obtained after SDS-PAGE of the purified protein extract from redcrest and padisarah.
7. Will denaturation change the primary sequence of the proteins? Why or why not? 8. Why was distilled water included in the samples tested?
3 i. Define Biological Value (BV) of Proteinsii. What are the advantages of this protein evaluation method when compared to Nbalance and chemical score?5iii. A bull consumes 7 kg DM of feed containing 60 g N/kg. The bull excretes 120 g N inthe faeces and 50 g N in the urine. The feacal and urinary N had 20 g metabolic feacalnitrogen (MFN) and 6 g endogenous urinary nitrogen (EUN) respectively.Calculate the BV of the protein in the diet.
i. What are the advantages of biological value of protein method compared to N-balance and chemical score? ii. A bull consumes 7 kg DM of feed containing 60 g N/kg. The bull excretes 120 g N in the faeces and 50 g N in the urine. The feacal and urinary N had 20 g metabolic feacal nitrogen (MFN) and 6 g endogenous urinary nitrogen (EUN) respectively. Calculate the BV of the protein in the diet.

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