Answered: Question 1. The ε-amino group of Lys…

Question 1. The ε-amino group of Lys has a pKa-value of 10.0; α-COOH = 2.2; α-NH3 = 9.0 Calculate the percentage of the ionic species which is protonated in a dilute Lys solution a) at pH 9.2.

Chemistry: Principles and Reactions

8th Edition

ISBN:9781305079373

Author:William L. Masterton, Cecile N. Hurley

Publisher:William L. Masterton, Cecile N. Hurley

Chapter23: Organic Polymers, Natural And Synthetic

Section: Chapter Questions

Problem 44QAP: A 1.00-mg sample of a pure protein yielded on hydrolysis 0.0165 mg of leucine and 0.0248 mg of...

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A 1.00-mg sample of a pure protein yielded on hydrolysis 0.0165 mg of leucine and 0.0248 mg of isoleucine. What is the minimum possible molar mass of the protein? (MMleucine=MMisoleucine=131g/mol)
(b) Describe how the charge of some amino groups in a protein might differ at pH 9.0 and pH 5.0. the charge on the amino group will differ at pH 5 and pH 9 which will depend on the pKa of the amino acid. (c) Describe how the charge of some carboxyl groups in a protein might differ at pH 9.0 and pH 5.0. charge on carboxyl group will differ at pH 5 and pH 9 which will depend on the pKa of the amino acid. (d) Given your answers to parts (b) and (c), what kind of intramolecular interactions in beta-galactosidase are most likely to be affected by a change in pH from 9.0 to 5.0? (e) Could the interactions you mention in part (d) affect the catalytic activity of beta-galactosidase?
In 0.1M solution glycine (pKa 9.6) at pH of 9.0, what fraction of glycine has its amino group in the -NH3+ form?
Valine has pKa's of 2.286 and 9.719. Estimate the fractional composition of Valine in the -1 form at pH=6.
4b) Canavanine is closely related to arginine, and like arginine its side group has a +1 charge when protonated. If you dissolved canavanine in an aqueous solution at pH 10, what would the net charge on a molecule of canavanine be? Please show your work or make it clear how you determined the charge contribution from each ionizable group.
Give typed solution only Which of the amino acids shown represents the structure of Ile at pH 10?
The pKa for the side chain amino group in lysine is 10.4. If we were working at physiological pH 7.4, what would be the ratio of the protonated to unprotonated versions of lysine? a. 1000:1 b. 3:1 c. 1:1000 d. 1:3
Explain why the pI of lysine is the average of the pKa values of its two protonated amino groups.
What is the name of this oligopeptide? Use the three letter and one letter nomenclature of the amino acids. Based on the charges on the peptide, what is the closest pH range would you expect that this was in? 2 to 4? 6 to 8? 10 to 12?
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Which amino acid has a net charge of +0.09 at pH 7? Show all calculations. Draw the structure of the amino acid that would predominate at this this pH. Circle all atoms that can be involved in making hydrogen bonds at pH 7
Finally, you want to make completely certain that you purified the correct protein and not some other protein (like biochemisnotfunase). To confirm the identity of your protein, you run a Western blot. When doing a Western, one typically needs a solution of phosphate-buffered saline, which is comprised of 10 mM phosphate buffer(pH 8.0) and 0.9% (w/v) NaCl. Describe how you would make 500 mL of this solution including the grams of sodium phosphate, monobasic and sodium phosphate, dibasic that you would need. Making the phosphate buffer is a little tricky. Be sure to use the correct ratio of monobasic and dibasic sodium phosphate to get the correct pH. The Henderson- Hasselbalch equation might come in handy here. Finally, the molecular weight of sodium phosphate, monobasic (NaH2PO4) is 119.98 g/mol and the molecular weight of sodium phosphate, dibasic (Na2HPO4) is 141.96 g/mol.