the pH of the resulting solution?4) Amino acids are polyprotic weak acids and are commonly used as biochemicalbuffering agents. You titrate NaOH into an aqueous solution of arginine with an initialpH of 1.0. Draw a titration curve demonstrating the expected pH change versusequivalents of NaOH added.5) Considering your titration curve from Question 4, draw the expected structure for themajor form of arginine at the FULL equivalent points (0, 1, 2, and 3).

pH = 1/Log [H+]If [H+] concentration in a solution is high, pH will be low and the solution is…

Answered: 4) Amino acids are polyprotic weak…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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1. What is the possible identity of the AA? a. Aspartic acid b. Lysine c. Alanine d. Proline 2. What is the isoelectric point of AA? 3. What is the pKa responding to the dissociation of the alpha-carboxylic group?
the enzyme LCK catalyzes the hydrolysis of the peptide KEY in 5.0 mM phosphate buffer at pH 7.0. The enzyme is known to obey Michaelis-Menten Kinetics. Under the conditions of this experiment: Vmax= 10 mmol/min/mg Km (KEY) = 0.20 mM Draw the complete structure of the tripeptide KEY and calculate its molecular weight Sketch the titration curve of the above tripeptide and label it.Determine the net charge of the peptide at each pk value Calculate the PI pf the peptide and draw the structure of the peptide at the isoelectric point.
A purified protein fraction has a total sample volume of 450 µL. The sample has a corrected A280 of 0.244, and the blank corrected A280 was 0.077. (Both values were measured with a path length of 1.00 cm.) If 5.50 µL of the sample was used in a reaction, calculate the mass of protein in the reaction (in µg).
Please draw titration curves for peptide HFDTYA and HEKDGQ, and calculate the pl for each. Usethis information to explain why the peptide HFDTYA has low solubility and HEKDGQ has a highersolubility in bulk water at pH = 7.
After staining an SDS-PAGE gel with Coomassie Blue G-250, the protein bands are visualized by de-staining the gel in a Coomassie Blue G-250 de-staining solution. This solution is made up of 10% acetic acid, 50% methanol, and 40% distilled water. How much of each of these components do you need to prepare 5 liters of Coomassie Blue G-250 de-staining solution?
6
An enzyme uses a lysine and a histidine as general acid-base catalytic residues. In one direction of the reaction, the lysine and histidine residues are typically protonated (~NH3*, ~Im), but in the other direction of the reaction, the two residues are "reverse protonated" (~NH2, ~Hlm*) (see below scheme). A pH profile of the reaction at various pH values yielded estimates of 7.57 and 9.30 for the macroscopic ionization constants pk,' and pK2, respectively. A separate set of experiments with site-speciffic variants of the enzyme yielded an estimate of 8.78 for the microscopic ionization constant pKp. Given this information, what is the value of the microscopic ionization constant pKA? Report your answer to the nearest hundredth. Lys-NH3* His-HIm" KB H KA H* Lys-NH2 Lys-NH3* His-HIm" His-Im Kc H* Kp Lys-NH2 His-Im
Calculate tthe ph of 50.0 mLs of 0.10 M arginine to which 20.0 mLs of 0.10 M HCL have been added.
1) Indicate the total charge of the peptide at pH 7.0, 9.0, and 11.0 2) Determine the isoelectric point (pI) for this peptide. Show the relevant pKa’s and your calculation. 3) What is the fraction of the peptide that has the N-terminal amino group deprotonated at pH 9.
The peptide aspartyl-glutamyl-leucyl-threonyl-alanine, shown in the sketch drawing window, has several ionizable groups. Adjust the charges to show the molecule as it would exist at pH 5.00. Use the pk values in the table below. pK, Values for Ionizable Groups of Amino Acids. Amino Acid pA, of a-COOH pA, of e-NH, pA, of Side Chain Isoelectric Point (pI) Alanine 235 9.87 6.11 Arginine 2.01 9.04 12.48 10.76 Asparagine 2.02 8.80 5.41 Aspartic acid 210 9.82 3.86 298 Cysteine 2.05 10.25 8.00 5.02 Glutzmic acid 2.10 9.47 4.07 3.08 Glutamine 217 9.13 5.65 Glycine 235 9.78 6.06 Histidine 7.11 9.18 6.10 7.64 Isoleucine 232 9.76 6.04 Leucine 233 9.74 6.04 Lysine 218 8.95 10.53 9.74 Methionine 2 28 9.21 5.74 Phenylalanine 2 58 9.24 5.91 Proline 2.00 10.60 6.30 Serine 221 9.15 5.68 Threonine 2.09 9.10 5.60 Trуptophan 238 9.39 5.88 Tyrosine 2 20 9.11 10.07 5.63 Valine 2 29 9.72 6.00 • Use the wedge hash bond tools to indicate stereochemistry where it exists. • If a group is 2chiral, do not use…
4 This is a three-part question about a tripeptide. Answer all three sub-questions. The pKR of side chains of Tyr, and Lys is 10.46 and 10.54 respectively. The molecular weight of amino acids Ala, Lys, and Tyr in neutral form is 89.1, 146.2, and 181.2 Da, respectively. 1) Draw the chemical structure of the dominant form of tripeptide AKY at pH = 11.5, ensure you have the correct stereochemistry and ionization state of each functional group (Hint, lysine has a C-epsilon as the furthest carbon from C-alpha). 2) Calculate the pI of tripeptide AKY, assuming the terminal amino group has a pKa of 8.0, and the terminal carboxyl group has a pKa of 3.5 3) Calculate the molecular weight of AKY at pI
A purified protein fraction has a total sample volume of 360 µL. The sample has a corrected A280 of 0.484, and the blank corrected A280 was 0.052. (Both values were measured with a path length of 1.00 cm.) If 5.00 µL of the sample was used in a reaction, calculate the mass of protein in the reaction (in µg).

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