10. Explain the difference at the molecular level in how temperature and urea denature a protein.

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
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10:16 AM Fri Sep 2
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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 >
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