## Part C: Calculating the Isoelectric Point (pI) for DTLH### Instructions:Using the pKa values provided in the table below, calculate the isoelectric point (pI) for the amino acid sequence DTLH.### Properties of Some Amino Acids Found in Proteins| Name | Abbreviations: 1- and 3-letter codes | pKa of α-COOH Group | pKa of α-NH₃⁺ Group | pKa of Ionizing Side Chain ||--------------|--------------------------------------|---------------------|---------------------|----------------------------|| Aspartic acid| D, Asp | 2.1 | 9.8 | 3.9 || Histidine | H, His | 1.8 | 9.2 | 6.0 || Leucine | L, Leu | 2.4 | 9.6 | - || Threonine | T, Thr | 2.6 | 10.4 | - |### Task:Express your calculated pI answer to two significant figures.### Submission:Enter your answer in the provided input box and press "Submit" to check your response.

Answered: Image /qna-images/answer/180778cc-2050-40ee-9257-11f70e26e5da.jpg

Answered: Using the values of pKas in the table…

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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Consider a protein in which a negatively charged glutamic acid side chain (pKa=4.2) makes a salt bridge (ion-ion interaction) with a positively charged histidine side chain (pKa=6.5). Part C: Justify your answer with calculations of partial charges on these amino acid side chains at pH=7.9.(Hint: Consider lessons from Coulomb's law, and the Henderson-Hasselbalch equation.)
α-Keratin is an intermediate filament with a basic structural unit of two a helices in a coiled coil. Each helix has a seven-residue repeating unit (heptad repeat). A representation of the a helices of a coiled coil dimer is shown. Each letter represents a different amino acid residue. f g d e Review the table of amino acids. a d g f Identify the three true statements about the structure of keratin. ☐ The a helix of the coiled coil is wound less tightly than predicted for an α helix. ☐ Each polypeptide in the dimer has 3.6 residues per turn, and a nonpolar group occurs every 3.5 residues, resulting in a slight winding, or twist, around the other polypeptide, forming a coiled coil. Arg-Ala-His-Glu-His-Thr-Asp is a likely repeat in the a helix of keratin. ☐ Val-Thr-Asp-Ala-Glu-Arg-His is a likely repeat in the a helix of keratin. ☐ The residues at positions b and c are less likely to be polar or charged because they are in contact with the solvent. ☐ Keratin molecules are very strong due…
Indicate the net charge of cysteine at pH 9.5 Express your answer using two significant figures.
0ミレーNレ NH geometry on both cand N. Torigonal plannes CH - C-N o=), HN CH2 CH-C-OH (a- carbon) CH2 HooC Aspaxagine - Toline - Valine - Arginine - phenylalcmine - Glutamic ocid. 1.Give the name and three letter code for each amino acid in the peptide. e 2. At pH 7, approximately what charge would be on your peptide? Explain your answer. 3. Can your peptide form intra/interchain disulfide bonds? Explain why/why not. e 4. Will your peptide absorb UV and is it fluorescent? Explain why/why not. e 5. What is the probability that your peptide contains a cis peptide bond? Explain your answer.
Given the following pKa data for the individual amino acids, estimate the pI for the tripeptide Thr-Asp-Arg. N-terminal amino group = 9.10 Side chain of aa #1 = Side chain of aa # 2 = 3.86 Side chain of aa # 3 = 12.48 C-terminal carboxyl group = 2.01 PI =
Discuss the reaction conditions you would need to carry out the PEGylation reaction of this peptide and explain how the pH affects the selectivity of these reactions.
What is the fraction of the peptide that has the N-terminal amino group deprotonated at pH 9. Please show your answer as a percent of deprotonated N-terminal species relative to all (protonated and deprotonated) N-terminal species. Can you show your calculations so I can understand your method of approach?
Identify and encircle the peptide bonds in this polypeptide (Asp-Sec-Leu-Cys-Glu).
For each amino acid, show the structure, 1-letter abbreviation, 3-letter abbreviation, class (non-polar, polar, positive or negative), special props, side chain pKa)
A cytosolic protein has an important alpha amino group. The pKa of this group is approximately 8 when exposed to water outside of a protein. 1. What would happen to the pKa if this group was instead buried in the hydrophobic interior of the protein? Explain. 2. Let’s say in the hydrophobic interior of the protein, the group forms an ionic bond with a carboxylate group of the side chain of a charged Asparagine residue. How would the pKa of this alpha amino group compare with the pKa of the alpha amino group in the hydrophobic interior of the protein without a nearby Asparagine residue to form this ionic bond? Explain.
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a. Suppose that you have the peptide Ala-Gly-Tyr-His-Leu and you treat it with FDNB and then 6M HCl. Draw the structures of all the products that you will have in solution (assume all reactions to go to completion).

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