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Consider a 0.203 L solution of the amino acid aspartic acid (0.615 M), which has an...
help with this question Consider a 0.211 L solution of the amino acid aspartic acid (0.631...
help with this question
Consider a 0.211 L solution of the amino acid aspartic acid (0.631 M), which has an alpha carboxylic acid group (pka = 2.10), an alpha amine group (pka = 9.82), and a carboxylic acid group in the side chain (pka = 3.86). If the titration is started at a very low pH, how many liters of 2.25 M NaOH would you need to add to reach the isoelectric point of the amino acid? Give your answer...
1A solution of 0.235 M aspartic acid, the charge neutral form of the amino acid, is...
1A solution of 0.235 M aspartic acid, the charge neutral form of the amino acid, is titrated with 0.118 M NaOH . The p K a values for aspartic acid are 1.990 , 3.900 , and 10.002 , corresponding to the α-carboxylic acid group, the β-carboxylic acid group, and the amino group, respectively. Calculate the pH at the first equivalence point of this titration.
Aspartic acid has three pKa values, 2.09, 3.86 and 9.82. a. On the following structure for...
Aspartic acid has three pKa values, 2.09, 3.86 and 9.82. a. On the following structure for this amino acid circle the protons that can be removed and indicate the corresponding pKa value? b. Determine the value of the isoelectric point for this amino acid. c. Sketch the structure of the zwitterion. d. If electrophoresis is carried out at pH is 7.0, will this amino acid migrate to the anode(+) or cathode(-).
At a pH of 4: Amino acid 1 OH Amino acid 2 NH OH HN NH,...
At a pH of 4: Amino acid 1 OH Amino acid 2 NH OH HN NH, OH pka Amino Amino Acid 1 Acid 2 9.82 9.18 Amino terminus Carboxy terminus 2.1 1.77 Side chain 3.86 6.1 O (Answer B) the R group (side chain) on amino acid 1 will be deprotonated A and B (Answer A) the amino terminus on amino acid OH HN OH pka Amino Acid 1 Amino Acid 2 Amino terminus 9.82 9.18 Carboxy terminus 2.1 1.77...
Plot the titration curve of aspartic acid it has a volume of
Plot the titration curve of aspartic acid it has a volume of \(100 \mathrm{ml}\) and \(0.1 \mathrm{M}\) when titrated with \(0.1 \mathrm{M}\) KOH? \(p k a 1=2.09, p k a 2=3.86\)\(\mathrm{pka} 3=9.82 ?\)
5. D-sorbital is found in 'sugar-free' chewing gum. It is formed by reducing D-glucose with NaBH Draw the structure of D-sorbital. s. (4 pts) Classify the following amino acid as polar, n...
5. D-sorbital is found in 'sugar-free' chewing gum. It is formed by reducing D-glucose with NaBH Draw the structure of D-sorbital. s. (4 pts) Classify the following amino acid as polar, non- polar, acidic, or basic: 6 (4 pts) The amino acid threonine (thr) has two chiral carbons. Draw a Fischer projection of the 2S,3S configuration of threonine. キ 7.(11 pts) Draw the tripeptide lys-asp-ser at physiological pH 8. (8 pts) The pK, values for aspartic acid are 2.10, 9.82...
Understand alpha helices and beta pleated sheets Question Every helical turn in an a-helix has 3.6 amino acid residues....
Understand alpha helices and beta pleated sheets Question Every helical turn in an a-helix has 3.6 amino acid residues. Then, hydrogen bonds are formed between the oxygen atom in amino acid along the the carbonyl group in the first amino acid and the hydrogen atom in the amine group of the chain. Select the correct answer below: third second fourth fifth FEEDBACK MORE INSTRUCTION SUBMIT Content attribution
(1) The following diagram represents a titration curve of histidine as pH increases; pKa = 1.82 represents the terminal carboxylic acid group. pK, represents the terminal amino group: 6.0 r...
(1) The following diagram represents a titration curve of histidine as pH increases; pKa = 1.82 represents the terminal carboxylic acid group. pK, represents the terminal amino group: 6.0 represents the R-group, and pK, E 9.17 7.59 pH 182 3.0 20 10 H (equivalents) At what point on the diagram is histidine predominantly present as the following species? COO A, at pH < 1.82 B. between pH 1.82 and pH 6.0 C) between pH 6.0 and pH 9.17 D. at...
Draw the titration curve for the titration of 20 mL of a 0.12 M solution of...
Draw the titration curve for the titration of 20 mL of a 0.12 M solution of glutamate (carboxylic acid pKa = 2.19, amino pKa = 9.67, you need to know the pKa for the R group) with 0.10 M sodium hydroxide. Clearly label the axes of your graph (pH vs mL of NaOH added.) Be sure to include pH values and volumes for the following: Start of the titration (no sodium hydroxide added), the pH at the volume that is...
2. The structure of the solid phase Wang resin linker and the first amino acid that we will use i...
2. The structure of the solid phase Wang resin linker and the first amino acid that we will use in this lab is shown below Fmoc first amino acid linker a) (1 pt) If the resin has 0.72 mmol/g of this linker on the surface of the beads, and you use 300 mg of resin for the reaction, how many mmol of linker do you have? b) (3 pts) All peptides will use alanine at the C-tenminus (position 1), Fmoc-L-valine...
help with this question
Consider a 0.211 L solution of the amino acid aspartic acid (0.631 M), which has an alpha carboxylic acid group (pka = 2.10), an alpha amine group (pka = 9.82), and a carboxylic acid group in the side chain (pka = 3.86). If the titration is started at a very low pH, how many liters of 2.25 M NaOH would you need to add to reach the isoelectric point of the amino acid? Give your answer...
At a pH of 4: Amino acid 1 OH Amino acid 2 NH OH HN NH, OH pka Amino Amino Acid 1 Acid 2 9.82 9.18 Amino terminus Carboxy terminus 2.1 1.77 Side chain 3.86 6.1 O (Answer B) the R group (side chain) on amino acid 1 will be deprotonated A and B (Answer A) the amino terminus on amino acid OH HN OH pka Amino Acid 1 Amino Acid 2 Amino terminus 9.82 9.18 Carboxy terminus 2.1 1.77...
Plot the titration curve of aspartic acid it has a volume of \(100 \mathrm{ml}\) and \(0.1 \mathrm{M}\) when titrated with \(0.1 \mathrm{M}\) KOH? \(p k a 1=2.09, p k a 2=3.86\)\(\mathrm{pka} 3=9.82 ?\)
5. D-sorbital is found in 'sugar-free' chewing gum. It is formed by reducing D-glucose with NaBH Draw the structure of D-sorbital. s. (4 pts) Classify the following amino acid as polar, non- polar, acidic, or basic: 6 (4 pts) The amino acid threonine (thr) has two chiral carbons. Draw a Fischer projection of the 2S,3S configuration of threonine. キ 7.(11 pts) Draw the tripeptide lys-asp-ser at physiological pH 8. (8 pts) The pK, values for aspartic acid are 2.10, 9.82...
Understand alpha helices and beta pleated sheets Question Every helical turn in an a-helix has 3.6 amino acid residues. Then, hydrogen bonds are formed between the oxygen atom in amino acid along the the carbonyl group in the first amino acid and the hydrogen atom in the amine group of the chain. Select the correct answer below: third second fourth fifth FEEDBACK MORE INSTRUCTION SUBMIT Content attribution
(1) The following diagram represents a titration curve of histidine as pH increases; pKa = 1.82 represents the terminal carboxylic acid group. pK, represents the terminal amino group: 6.0 represents the R-group, and pK, E 9.17 7.59 pH 182 3.0 20 10 H (equivalents) At what point on the diagram is histidine predominantly present as the following species? COO A, at pH < 1.82 B. between pH 1.82 and pH 6.0 C) between pH 6.0 and pH 9.17 D. at...
2. The structure of the solid phase Wang resin linker and the first amino acid that we will use in this lab is shown below Fmoc first amino acid linker a) (1 pt) If the resin has 0.72 mmol/g of this linker on the surface of the beads, and you use 300 mg of resin for the reaction, how many mmol of linker do you have? b) (3 pts) All peptides will use alanine at the C-tenminus (position 1), Fmoc-L-valine...
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