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%
What percent of glutamic acid with a pKR of 4.25 has a protonated r-group at a...
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?
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
The pK of the side chain carboxyl group of glutamic acid is 4.3. What is the ratio of charged to uncharged forms of this group at pH 7.3? explain with work
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.
Glutamic acid (shown below) has a pi of 3.2. What is the structure of glutamic acid at pH = 10? H3N H3N 02H H2CO2 CO2H لم CO2H HaN H2N Hanco 0H coo H₂N
Glutamic acid (shown below) has a pI of 3.2. What is the structure of glutamic acid at pH = 10? O2 C2H НEN сон .Соон HзN НзN сон CO2H H2N со-н H2N H2N
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...
#1) a) The pK1, pK2, and pKR for the amino acid histidine are 1.8, 9.3, and 6.0, respectively. At pH 4.0 would be charged predominantly as follows: A a-carboxylate 0, a-amino +1, imidazole +1, net charge +2 B a-carboxylate +1, a-amino +1, imidazole −1, net charge +1 C a-carboxylate −1, a-amino +1, imidazole 0, net charge 0 D a-carboxylate +1, a-amino 0, imidazole −1, net charge 0 E a-carboxylate −1, a-amino +1, imidazole +1, net charge +1 b) The pK1,...
The triprotic form of the amino acid glutamic acid is shown below, along with the pK, value for each ionizable site. B 9.7 l A 2.2 +H3N— C—C—OH c= 0 OH C 4.3 In the monoprotic form of the molecule, is each of the sites (labeled A, B, and C) protonated or unprotonated? site A:( site B: site C: The triprotic form of the amino acid arginine is shown below, along with the pK, value for each ionizable site. B...
A mixture of arginine, glutamic acid, and leucine is applied to the center of an electrophoresis plate. After the pH is adjusted to 6.0 and an electric current is applied, the components of the mixture separate. Which of the following describes the plate after the experiment has been completed? A. Leucine migrates towards the negative electrode, arginine migrates towards the positive electrode, and glutamic acid stays near the center. B. Glutamic acid migrates towards the negative electrode, arginine migrates towards...