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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

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

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 >
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