1. Draw an approximate titration curve of the following amino acid. Label the approximate isoelectric point ofarginine on the curve and be sure to label the axis of the graph appropriately. You DO NOT need to draw thestructure of this amino acid here. Pk1= 1.92, pk2=8.99 and pk3=12.48. Show your work for determining theisoelectric point. You can draw out your curve within the text box or upload a drawing.A▾B I-IB 7

The titration curve is a plot that tracks the behavior of amino acids under the influence of…

Answered: 1. Draw an approximate titration curve…

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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Similar questions

use one-letter code for amino acid if needed what is the overall amino acid sequence?
For the following amino acids select the INCORRECT alternative: (a) At pH = 4 all migrate towards the cathode except Asp. (b) At pH = 10 all migrate towards the anode. (c) The pI of phenylalanine (Phe) will be about 5.5. (d) The pl of aspartic acid (Asp) will be about 2.8. (e) At pH = 7 the amino acids Arg and Lys migrate towards the cathode and the rest to the anode.
A sample mixture consists of three proteins with the following properties: Protein A MW (kDa) 200 Amino acid composition 40% nonpolar, 60% polar B 45 20% nonpolar, 80% polar C 98 85% nonpolar, 15% polar IpH 9 3 5 1. If the mixture is subjected to ammonium sulfate precipitation, which protein will precipitate out first? [Select] 2. If the mixture is subjected to isoelectric focusing, which protein will stop moving nearest to the positive electrode? [Select] 3. If the mixture is subjected to cation-exchange chromatography using a buffer at pH 7, which protein will bind to the resin? [Select] 4. If the mixture is subjected to SDS-PAGE, which protein will be at the bottommost portion of the gel? [Select] * Previous Nex
B) An aqueous solution (pH ~7) containing mixture of three amino acids; glycine (G), arginine (R) and glutamic acid (E), was dropped onto center of a solid matrix (e.g chromatographic paper) which is incorporated in an electrical circuit (a). After applying electrostatic potential, the aminoacids are separated as shown in b. Determine amino acids that are labeled as 1, 2 and 3. a) DC Power Supply (OFF) b) DC Power Supply (ON) Solid matrix Solid matrix Cathode Anode Cathode Anode buffer buffer buffer buffer Sample containing amino acids G, R, E
what is the n-terminal AA residue? use one-letter code for amino acid
1. Amino acid analysis of the peptide gave the following residues: Asp Leu Lys Met Phe Tyr. The following facts were observed: Trypsin treatment had no effect. The phenylthiohydantoin released by Edman degradation was C-C-CH2. Brief chymotrypsin treatment yielded several products including a dipeptide and a tetrapeptide. The tetrapeptide contained Leu, Lys and Met is some order. Cyanogen bromide treatment afforded a dipeptide, a tetrapeptide and a free Lys. What is the amino acid sequence for this heptapeptide?
Please be clear in your explanation. I need to figure out how to find the pI of the amino acid. Thank you!
You will now build a 15 amino acid peptide using another paper or wire backbone as you did above. You will pick 15 amino acids, matching the criteria below, and put them onto your backbone about 3 inches apart. This will be the primary structure of your novel protein. Select 15 amino acids that meet the following criteria 6 hydrophobic R groups 2 acidic R groups 2 basic R groups 2 cysteine R groups 3 hydrophilic R groups Place the R groups in any order you choose on your paper or wire backbone as you did above. Start at the N-terminus and place each R group about 3 inches apart until all 15 are attached to the mini toolbar. You have just built the primary structure of your protein. Question 1: Record the sequence of amino acids in your protein, starting with the N-terminus. The N-terminus is the end of the polypeptide that has a free nitrogen group. The C-terminus, or carboxyl end, will have a free carboxyl group. You can use the three letter amino acid abbreviation to…
Draw the L enantiomer in a Fischer projection for each amino acid; identify the amino acid as neutral, acidic, or basic. Give the three-letter sign [3], and the one-letter symbol [4].arginine a. arginine b. arginine c. a. glutamic acid b. glutamic acid c. glutamic acidtyrosine b. valine c. arginine
For the following pentapeptides: Ser-Glu-Gly-His-Ala and Gly-His-Ala-Glu-Ser A. Compute their isoelectric pH (pI). Show full solution. Use standard pKa values. B. Do these peptides with the same amino acid composition have different net charges at pH 7.0? Explain briefly. C. Would you expect the titration curves of the two peptides to differ? Why or Why not?
Patients suffering from sickle cell anemia have a mutation in the gene that codes for one of the hemoglobin chains, in which a single glutamate is replaced by a valine. Propose an explanation for why this substitution has such a striking effect on protein structure and function with explanation. Suggest two other amino acids that would be less likely to cause such serious impairment of hemoglobin function if each was substituted for glutamate. Briefly explain your answer.
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?

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