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11. Based on the denaturation curve shown here for two separate proteins, A and B: a. Label the y-axis: b. Which protein is more stable? Why? c. Other than urea concentration, what is another potential parameter for the x-axis? Protein A VA Protein B 1.0 0.8- 0.6- 0.4 0.2 0.0 Urea concentration (M)

11. Based on the denaturation curve shown here for two separate proteins, A and B: a. Label the y-axis: b. Which protein is more stable? Why? c. Other than urea concentration, what is another potential parameter for the x-axis? Protein A VA Protein B 1.0 0.8- 0.6- 0.4 0.2 0.0 Urea concentration (M)

Biochemistry
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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10:16 AM Fri Sep 2 < то 8. Predict the effect of each of the following environmental changes on the pKa of a glutamate side chain and explain your logic. The N-terminus of the protein is brought into the proximity of glutamic acid A lysine side chain is brought into the proximity of glutamic acid the glutamic acid side chain is shifted from the outside of the protein to the interior 9. A small protein was completely hydrolyzed and found to contain (in no particular order): Arg, Cys, Lys, Met, Phe, Thr, a. Incubation with FDNB generated Sanger Reagent yielded DNP-Lys b. Incubation with chymotrypsin had no effect on the peptide c. Incubation with trypsin yielded free arginine and lysine d. Incubation with cyanobromide yielded a tetrapeptide capable of disulfide bonding. 10. Explain the difference at the molecular level in how temperature and urea denature a protein. 11. Based on the denaturation curve shown here for two separate proteins, A and B: a. Label the y-axis: b. Which protein is more stable? Why? c. Other than urea concentration, what is another potential parameter for the x-axis? b) Chaperone Proteins: c) Protein Domain: 1,0 d) Protein Data Bank: 0.8- 0.6 0.4- 0.2 12. Define the following (note: you my need to use internet resources to do so): a) Native state: 0.0 @83% +: Protein A A Protein B Urea concentration (M) < WIN >
Transcribed Image Text:10:16 AM Fri Sep 2 < то 8. Predict the effect of each of the following environmental changes on the pKa of a glutamate side chain and explain your logic. The N-terminus of the protein is brought into the proximity of glutamic acid A lysine side chain is brought into the proximity of glutamic acid the glutamic acid side chain is shifted from the outside of the protein to the interior 9. A small protein was completely hydrolyzed and found to contain (in no particular order): Arg, Cys, Lys, Met, Phe, Thr, a. Incubation with FDNB generated Sanger Reagent yielded DNP-Lys b. Incubation with chymotrypsin had no effect on the peptide c. Incubation with trypsin yielded free arginine and lysine d. Incubation with cyanobromide yielded a tetrapeptide capable of disulfide bonding. 10. Explain the difference at the molecular level in how temperature and urea denature a protein. 11. Based on the denaturation curve shown here for two separate proteins, A and B: a. Label the y-axis: b. Which protein is more stable? Why? c. Other than urea concentration, what is another potential parameter for the x-axis? b) Chaperone Proteins: c) Protein Domain: 1,0 d) Protein Data Bank: 0.8- 0.6 0.4- 0.2 12. Define the following (note: you my need to use internet resources to do so): a) Native state: 0.0 @83% +: Protein A A Protein B Urea concentration (M) < WIN >
Expert Solution
Step 1

The 3-dimensional structure of a protein is dependent on the non-covalent interactions such as hydrogen bonding, hydrophobic interaction, electrostatic interaction and van der Waals interaction. 

The treatment of a protein with a chemical denaturant disrupts the noncovalent interactions resulting in the unfolding of the protein.

The protein denaturation curves obtained with different proteins can be used for the comparison of their stability. 

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