A 100 mL of 0.1 M amino acid at pH 1.0, whose pka for the carboxyl group is less than the pKa of the R-group, was titrated with NaOH solution. The pH wasmonitored, and the results were plotted on a graph, as shown below. The key points in the titration are designated A to G.12108pH 6420AB0.5сDEF1.522.5Equivalents of OH1. What is the possible identity of the amino acid? [Select]2. What is the isoelectric point of the amino acid? [Select]3. What is the pka corresponding to the deprotonation of the alpha-amino group? [Select]4. Region/ point where the amino acid is predominantly present as a (-2)-charged species. [Select]5. The effective buffering range for the amino acid in the basic region. [Select]G3

The amino acids carry different ionizable groups. The ionic form of the amino acids depends upon the…

Answered: A 100 mL of 0.1 M amino acid at pH 1.0,…

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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80mL of a 0.3M solution of hexapeptide Leu-His-Cys-Glu-Asn-Arg is adjusted to pH=pl. The solution is then titrated with 0.2M HCI to a final pH of 2.1. Sketch the titration curve, labelling the pH and volume axes. Indicate the volume of HCl needed to reach each relevant pKa value and equivalence point(s). Relevant pka values are: 2.1, 4.3, 6.0, 8.3, 9.8, and 12.5.
80mL of a 0.3M solution of hexapeptide Leu-His-Cys-Glu-Asn-Arg is adjusted to pH=pI. The solution is then titrated with 0.2M HCL to a final pH of 2.1. Sketch the titration curve, labelling the pH and volume axes. Indicate the volume of HCL needed to reach relevant pKa value and equivalence point(s)z Relevant pKa values are: 2.1, 4.3, 6.0, 8.3, 9.8, and 12.5.
A 100 mL solution of 0.1 M glycine at pH 1.72 was titrated with 2 M LIOH. The pH was monitored and the result were plotted as shown in the graph. The key points of the titration are designated as I to V. Identify the key point in the titration corresponding to the pH at which the carboxyl group is half deprotonated. 12 JL30 (V) 9.60 (IV) 8 5.97 pH 6 2.34 CII) 2 (I) 0.5 1.0 1.5 2.0 OH (equivalents) IV O Il and IV Next
Five amino acids were subjected to normal phase chromatography, and the folowing Rf values were computed: A 0.59 В - 0.12 C- 0.71 D- 0.33 E - 0.20 Which is the most polar amino acid? O A O B
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).
Draw Haworth projection formulas for the b-anomer of monosaccharides with each of the following Fischer projection formulas
A stock solution contains 0.2 mg/mL protein. From this stock solution, 179 uL is diluted with 1.1 mL buffer. What is the concentration of protein in this dilution?
An enzyme (molecular weight= 24 kDa, pI= 5.5) is contaminated with two other proteins, one witha similar molecular mass and a pI of 7.0 while the other has a molecular mass of 100 kDa and a pIof 5.4. Suggest how the contaminated enzyme can be purified.
The amino acid glycine is often used as an ingredient in buffers for biochemistry experiments. The amino group of glycine has a pKa of 9.6. Glycine exists in either a protonated form (-NH3+) or a free base (-NH₂). a) In what pH range can glycine be used as an effective buffer? b) In a 0.1M solution of glycine at pH 9.0, what fraction has its amino group in the protonated form? c) When 99% of the glycine is in the protonated from, what is the numerical relation between the pH of the solution and the pKa of the amino group?
Sketch the titration curve for the amino acid alanine with pka1 = 2.34 and pka2 = 9.69.
Draw the titration curve for an 800 mL 0.25 M solution of Arginine. (Graph pH vs. mole OH-.) Where onthe curve is the charge on Arginine +1.5? Identify it on the graph.
A mixture of Asparagine (pl 5.41), Aspartic Acid (pl 2.98), Histidine (pl 7.59), Lysine (pl 9.74) and Threonine (pl 6.53) are separated by cation exchange chromatography. What is the order of elution of these amino acids if you use gradient buffer system from pH 10 to pH 2: v First 1. Asparagine v Second 2. Aspartic Acid 3. Histidine v Third 4. Lysine v Fourth 5. Threonine v Fifth 6. No separation

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