Each ionizable group of an amino acid can exist in one of two states, charged or neutral. The electric charge on the functionalgroup is determined by the relationship between its pKa and the pH of the solution. This relationship is described by theHenderson-Hasselbalch equation.aHistidine has three ionizable functional groups. Complete the equilibrium equations by assigning the proper pK₁ for eachionization and the net charge on the histidine molecule in each ionization state.H ||H₂N-C-C-OH|CH₂2+HN-1-NHpKa= 1.8+2||H₂N-C-C-0-1CH₂+HN-NHpKa = 9.17Answer BankpK₂ = 7.59H||H₂N-C-C-0-|CH₂NpKa-NH= 6.0-2н IIH₂N-C-C-0-|CH₂+1NC-NH0

If the pKa is low, the pH of the solution is less, and the acidity of the solution is high. i.e.,…

Answered: Each ionizable group of an amino acid…

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

Which of the twenty naturally occurring amino acid side chains are charged at a pan of 1.00? pH of 7.00? pH of 12.00? Make a table.
In case of the same amino acid as in the picture, in which ionization state would this amino acid be at (i) a pH that will correspond with the pI-value and (ii) a pH below the pI-value?
Phosphate buffers are commonly used to mimic biological systems. Given that phosophoric acid is a triprotic acid with three pKas (2.12, 7.21, and 12.32), why do you think this is? What are the dominant buffering compounds present in a phosphate buffer near physiological pH?
What is the contribution of dilsulfide bonds in proteins?Which groups or side chain participate in these reactions? Discuss with examples in detail.
What average positive charge of an amino acid side chain with pKa 10.9 at a pH value of 11.9? Answer up to two decimals. (Please type answer no write by hend)
1.0.1 mL of a protein solution of concentration of 11 mg/mL was diluted to a total volume of 4.0 mL with water (i.e. 0.1 mL of the solution was added to 3.9 mL of water). 2 mL of this solution was then mixed with 18 mL of water. What is the concentration of the diluted protein solution? Space to show your workings:
A tetrameric protein dissociates into dimers when the detergent sodium dodecyl sulfate (SDS) is added to a solution of the protein. But the dimers are termed SDS-resistant because they do not further dissociate into monomers in the presence of the detergent. What intermolecular forces might be acting at the dimer-dimer interface? Are the intermolecular forces acting at the monomer-monomer interface different? Explain.
A 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 separation
At 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 2.17
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 answer
the enzyme LCK catalyzes the hydrolysis of the peptide KEY in 5.0 mM phosphate buffer at pH 7.0. The enzyme is known to obey Michaelis-Menten Kinetics. Under the conditions of this experiment: Vmax= 10 mmol/min/mg Km (KEY) = 0.20 mM Draw the complete structure of the tripeptide KEY and calculate its molecular weight Sketch the titration curve of the above tripeptide and label it.Determine the net charge of the peptide at each pk value Calculate the PI pf the peptide and draw the structure of the peptide at the isoelectric point.
After staining an SDS-PAGE gel with Coomassie Blue G-250, the protein bands are visualized by de-staining the gel in a Coomassie Blue G-250 de-staining solution. This solution is made up of 10% acetic acid, 50% methanol, and 40% distilled water. How much of each of these components do you need to prepare 5 liters of Coomassie Blue G-250 de-staining solution?

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