The activity of an enzyme requires a glutamic acid to display its −COOH functional group in...
The activity of an enzyme requires a glutamic acid to display its −COOH functional group in the protonated state. Suppose the pKa of the −COOH group is 4.07. At what pH will the enzyme show 82% of maximal activity?
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The activity of an enzyme requires a glutamic acid to display
its −COOH functional group in...
The activity of an enzyme requires a cysteine to display its -SH side chain in the...
The activity of an enzyme requires a cysteine to display its -SH side chain in the deprotonated state. The pKa of the -SH group is 8.3. At what pH will the enzyme show 65.0% of maximal activity?
Suppose you are researching a special enzyme named "Generic Enzyme." Generic Enzyme has an amino acid...
Suppose you are researching a special enzyme named "Generic Enzyme." Generic Enzyme has an amino acid side chain functional group that must be in the protonated form for the enzyme to be active. You have just purified Generic Enzyme and found that 1 in every 4 individual Generic Enzyme molecules is active. Your special Generic Enzyme is at a pH of 7.75. Generic enzyme has a phenolic hydroxyl group which is responsible for its catalytic activity. What is the pKa...
Note that the pKa of gamma-carboxyl group of glutamic acid is: 4.3. Calculate the pH at...
Note that the pKa of gamma-carboxyl group of glutamic acid is: 4.3. Calculate the pH at which the gamma-carboxyl group of glutamic acid is 3/5 dissociated. What is the concentration of [H^+] in solution at this pH? Show your calculations to receive full credits.
Suppose you have a peptide composed of 4 amino acids bonded together: glutamine, glycine, glutamic acid,...
Suppose you have a peptide composed of 4 amino acids bonded together: glutamine, glycine, glutamic acid, and the novel amino acid friendsamine, which has an ionizable side group with a pKa of 5.9. At pH 7.0, this peptide has a net charge of -2. What is the charge on the protonated form of the friendsamine side group? Explain how you determined the charge on the protonated friendsamine side group
What percent of glutamic acid with a pKR of 4.25 has a protonated r-group at a...
What percent of glutamic acid with a pKR of 4.25 has a protonated r-group at a pH of 3.9 ? a. 50% b. 31% c. 74% d. 69%
1. (a) Draw the structure of L-glutamic acid and show its one letter and three letter...
1. (a) Draw the structure of L-glutamic acid and show its one letter and three letter code. (1 pt) (b) Show the calculation for its isoelectric point. (HINT: Check the pKa of the R group also.) (2 pt) (c) Draw the forms of glutamic acid at pH 1, 6 and 10. (3 pt) (d) To which electrode would glutamic acid migrate in electrophoresis at pH 7 buffer, the anode (+) or cathode (-)? (1 pt) (e) MSG (monosodium glutamate) is...
We have seen that amino acid residues Asp52 and Glu35 are required for lysozyme?s catalytic activity:...
We have seen that amino acid residues Asp52 and Glu35 are required for lysozyme?s catalytic activity: • Assume that the side chain pKas are the usual valuesof 3.90 for Asp and 4.07 for Glu. At pH 5.0 (the pH optimum for lysozyme) what proportion of enzyme molecules have both Asp52 and Glu35 in the correct ionization state? • Are the pKa values likely to be correct? What change in pKa might be present within lysozyme?
Enzyme X exhibits maximum activity at pH = 5.25. X shows a sharp decrease in its activity when th...
Enzyme X exhibits maximum activity at pH = 5.25. X shows a sharp decrease in its activity when the pH goes much lower than 4.35. One likely interpretation of this pH activity is that: A) a Glu residue (pKa = 4.25) on the enzyme is involved in the reaction. B) a His residue (pKa = 6.0) on the enzyme is involved in the reaction. C) the enzyme has a metallic cofactor. D) the enzyme is found in gastric secretions. E)...
Enzyme B has two arginine amino acid resídues that are responsible for catalysis. For catalysis one...
Enzyme B has two arginine amino acid resídues that are responsible for catalysis. For catalysis one arginine side chain is protonated and one is deprotonated. What is the optimal pH for Enzyme B activity? 2 4 6 10 12 please show
The effect of pH on the activity of an enzyme was examined. At its active site,...
The effect of pH on the activity of an enzyme was examined. At its active site, the enzyme has an Ionizable group that must be positively charged for substrate binding and catalysis to take place. The Ionizable group has a pk of 6.0. The substrate is negatively charged throughout the pH range of the experiment At what pH=9. the enzyme will be operating at answer is either Vmax, 1/2 Vmax or less than 1/2 Vmax (type in one of the...
Note that the pKa of gamma-carboxyl group of glutamic acid is: 4.3. Calculate the pH at which the gamma-carboxyl group of glutamic acid is 3/5 dissociated. What is the concentration of [H^+] in solution at this pH? Show your calculations to receive full credits.
The effect of pH on the activity of an enzyme was examined. At its active site, the enzyme has an Ionizable group that must be positively charged for substrate binding and catalysis to take place. The Ionizable group has a pk of 6.0. The substrate is negatively charged throughout the pH range of the experiment At what pH=9. the enzyme will be operating at answer is either Vmax, 1/2 Vmax or less than 1/2 Vmax (type in one of the...
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