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Problem Set 2 - on the SDS gel shown below What can you...

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Problem Set 2 BIBC 100 1. For each of the following amino acid substitutions, indicate if they would be apt to cause a change or disruption of protein structure and explain your answer. Ala to Gly Leu to Lys Asp to Glu Val to Tyr 2. You are interested in studying the effects of different environments on the activity of an enzyme you are working on in lab. How do you think each of the following environments would affect the activity of your enzyme? Explain your answer. If protein activity is disrupted, which types of interactions would be affected? a. Boiling water b. Sulfuric Acid c. Tris Buffer 3. Which of the following peptides do you think would form a more stable alpha helix and why? 1. A – V – R – M – W – V – E – L – S 2. R – K – R – W – Q – K – R – M - H – W 4. You add a reducing agent to a protein in lab and then run this protein sample
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Unformatted text preview: on the SDS gel shown below. What can you conclude about your protein? 10 kD 8 kD 6 kD 4 kD 2 kD 5. You have just completed a mass spectrometry experiment and you have successfully determined the molecular mass of your 100 amino acid protein. For the experiment, you treated your protein with the enzyme trypsin, which cleaves after all Lys and Arg residues. Your protein has Lys at positions 25, 65 and 82 and Arg at positions 14, and 58. a. How many amino acids would you have in each of the resulting proteolytic fragments? b. Estimate the molecular weight of each of these fragments. (Remember that the mass spec technique would give you exact masses of each of these fragments) c. What information do you gain by cleaving your peptide with trypsin?...
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