Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
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Question
Consider a peptide with the sequence Ala-Glu-Arg-Leu. Assume the ionizable groups have the pKa values listed in Table 2.1 of your text.
(a) Draw the predominant ionic form of the peptide at pH 7.4.
(b) Determine the net charge of the predominant form of the peptide at pH 7.4.
(c) Calculate the pI of the peptide.
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- 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, Earrow_forwardwhat is the n-terminal AA residue? use one-letter code for amino acidarrow_forwarddraw the primary structure of the polypeptide at physiological pH range of 7.35-7.45 using condensed structures 3-letter abbreviations with a hyphen representing peptide bond give the name of the peptide, determine the net charge, and calculate the isoelectric point KRINPLAarrow_forward
- Amino acid structure For any ionizable group, indicate the pka value and draw the structure that would be expected at the pH inside the cell (~7.4).arrow_forwardBased on the following image, what is the N-terminal AA residue, C-terminal AA residue? What is also the sequence of peptide 2 and peptide 3? Also identify the overall amino acid sequencearrow_forwardA 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 separationarrow_forward
- 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.arrow_forwardAt which pH would the peptide with the amino acid sequence 'KEYHR' be found in an IPG (Immobilized pH gradient) strip after successful isoelectric focusing. Show calculation. lonizable groups Alpha amine group of K Side chain group of K Side chain group of E Side chain group of Y Side chain group of H Side chain group of R Alpha carboxylic acid group of R pka 8.95 10.53 4.25 10.07 6 12.48 2.17arrow_forwardWhat is the net charge on the peptide RHTLE at pH 12.5?arrow_forward
- The amino acid arginine ionizes according to the following scheme: (a) Calculate the isoelectric point of arginine. You can neglect contributions from form I. Why? (b) Calculate the average charge on arginine when pH = 9.20. (c) Is the value of average charge you calculated in part b reasonable, given the pI you calculated in part a? Explain your answerarrow_forwardConsider the peptide Trp-Arg-Glu-Cys-Gly-Tyr. For the drawings requested below, please show them in zig-zag style, from amino to carboxy terminus, with correct stereochemistry Draw the predominant form at pH = 2 Draw the predominant form at pH = 5 Draw the predominant form at pH = 7 Draw the predominant form at pH = 12arrow_forwardPlease 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.arrow_forward
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