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?
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The activity of an enzyme requires a cysteine to display its -SH
side chain in the...
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?
The pKa of the cysteine side chain group is 8.32, so it is about 88.5% dissociated...
The pKa of the cysteine side chain group is 8.32, so it is about 88.5% dissociated at pH? What is the total net charge on asparigine at pH 9? Use correct sign and 3 decimal points in your answer.
1. Calculate the charge on the side chain of the amino acid histidine using the Henderson-Hasselbach...
1. Calculate the charge on the side chain of the amino acid histidine using the Henderson-Hasselbach equation pH = pKa + log (A/HA+). Use pH =7 and a pKa = 6 and solve to 2 significant figures. 2. Cysteine proteases have unusually reactive cysteine side chains. For one of these enzymes in solution at pH 7 you are able to measure the amount of the deprotonated sulfhydryl (ie, the negatively charged species) as 40% of the total. Calculate the pKa...
1) The pKa for the imidazole group in histidine in Papain's catalytic centers is 8.3. What...
1) The pKa for the imidazole group in histidine in Papain's catalytic centers is 8.3. What is the ratio of protonated and deprotonated His-R groups at pH 8.2? a) 5 NH+ / 4 N: b) 1 NH2+ / 1 NH c) 4 N: / 5 NH+ d) 1 NH / 1 NH2+ 2) What is the ratio of protonated vs deprotonated Cysteine sulfhydryl groups in the catalytic center of papain, pKa 3.4, at optimal pH of 6.2? a) 1 S-...
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...
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
13. (3 pt) An enzyme needs a specific lysine side- chain to be protonated to be...
13. (3 pt) An enzyme needs a specific lysine side- chain to be protonated to be active. What percentage of the enzyme will be active at pH 7 if the pKR of this lysine side-chain is 9.6? <1% 10% А. В. 75% >99%
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)...
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?
Question 30 (1 point) Saved If an amino acid with a nonionizable side chain has a...
Question 30 (1 point) Saved If an amino acid with a nonionizable side chain has a pka for its a-carboxyl group of 2.4 and a pka for its a-amino group of 9.8, what is its pl? 12.2 Not enough information 06.1 07.4
13. (3 pt) An enzyme needs a specific lysine side- chain to be protonated to be active. What percentage of the enzyme will be active at pH 7 if the pKR of this lysine side-chain is 9.6? <1% 10% А. В. 75% >99%
Question 30 (1 point) Saved If an amino acid with a nonionizable side chain has a pka for its a-carboxyl group of 2.4 and a pka for its a-amino group of 9.8, what is its pl? 12.2 Not enough information 06.1 07.4
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