All amino acids have two ionizable functional groups: an a-amino group (average pK, of 9.4) and an a-carboxylic acid group(average pK, of 2.2). Lysine also has an ionizable side chain (R group) with a pK, of about 10.5. One of the possible ionizationstates of lysine is shown in the image.iH₂N-CH-C-OHCH₂1IncorrectCH₂CH₂CH₂NH₂At what pH would the structure be the predominant ionization state? Consider the ionization state of all three of thefunctional groups.Show Transcribed Text11.9SThe protonated form of the R group of lysine is shown in the structure. The ratio of the charged (protonated) form to thedeprotonated form depends on the pK, of the R group and the pH of the solution.12.010.55.4Select all the pH values at which the charged form of the R group would predominate.2.2

They form the basic unit of the proteins. The acidity of the amino acids can be determined from…

The protonated form of the R group of lysine is shown in the structure. The ratio of the charged (protonated) form to the deprotonated form depends on the pK, of the R group and the pH of the solution. Select all the pH values at which the charged form of the R group would predominate. 12.0 10.5 5.4 2.2

The protonated form of the R group of lysine is shown in the structure. The ratio of the charged (protonated) form to the deprotonated form depends on the pK, of the R group and the pH of the solution. Select all the pH values at which the charged form of the R group would predominate. 12.0 10.5 5.4 2.2

Chemistry

10th Edition

ISBN:9781305957404

Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Chapter1: Chemical Foundations

Section: Chapter Questions

Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...

See similar textbooks

Similar questions

draw the structure of EDPTK in its predominant form as it would exist at pH 5
4. Proteases are enzymes that catalyze the hydrolysis of peptide bonds in proteins. The enzyme trypsin is a protease that specifically hydrolyzes only those peptide bonds that are formed by the carboxyl group of basic amino acid residues. Trypsin is present in the small intestine where it functions at an optimum pH of 8. Consider the pentapeptide Phe-His-Val-Lys-Glu. Draw the structures of the products formed from trypsin-catalyzed hydrolysis of this peptide.
The isoelectric point (pl) can best be calculated by: Averaging the sums of all pkas. Averaging the sum of the two pKas closest to physiological pH. Averaging the two pKas "sandwiching" the zwitterionic form. Averaging the two pKas of the alpha-amino and alpha-carboxy groups.
a) A solution of amino acid having carboxylic side chain was titrated against NaOH. If initial pH of the solution was 2.8. Describe the state of the functional groups of the amino acid at the initial pH and at 10.5.
what is The method that would be BEST to use to monitor protein secondary structure during the titration of a denaturing agent?
The R group of the amino acid Asp contains a carboxyl group with a pKa of 3.7. But the pka of the alpha-carboxyl group in Asp is 1.9. Which of the following. explanations could reasonably account for this difference? 3.7 is the isoelectric pH, which is estimated by averaging the pka of the alpha- carboxyl group with the much higher pKa of the alpha-amino group The R group of Asp also contains an NH2 group, which is less acidic than a carboxylic acid The conjugate base of the alpha-carboxyl could be stabilized by an attractive ionic interaction with the nearby alpha-amino group, which is protonated at low pH Water has better access to the R group than to the alpha-carboxyl group, so it more effectively solvates the charged form of the R group and stabilizes it
please help
Shown below is the amino acid tyrosine in its protonated state, with the pK of each ionizable proton indicated. pK = 10 HO H₂N pK = 9 COOH pK = 2 Which best represents the predominant state of tyrosine at pH 7? a HO b B C HO d HO Time left 0:20:16 H.N COOH HN COO HN COO HN COO
Peptides can be separated using an ion-exchange column based on their isoelectric (pl) values. At which pH values would two different peptides, one with a pl of 5.6 and the other with a pl of 9.1, bind to a cation- and anion-exchange column? Each peptide may be capable of binding to each column at more than one pH value. anion-exchange column at pH = 3.1 pH = 7.2 pH = 10.6 ****** cation-exchange column at pH = 3.1 pH = 7.2 PH =10.6 Answer Bank peptide B pl = 9.1 peptide A pl = 5.6
All amino acids have two ionizable functional groups: an α‑amino group (average pKa of 9.4) and an α‑carboxylic acid group (average pKa of 2.2). Aspartic acid has an ionizable side chain (R group) with a pKa of about 3.8. One of the possible ionization states of aspartic acid is shown in the image. At what pH would the structure be the predominant ionization state? Consider the ionization state of all three of the functional groups.
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
How does the shape of a titration curve confirm the fact that the pH region of greatest buffering power for an amino acid solution is around its pK's? Name four factors (bonds or other forces) that contribute to stabilizing the native structure of a protein, and describe one condition or reagent that interferes with each type of stabilizing force. Why is silk fibroin so strong, but at the same time so soft and flexible?