Essential Organic Chemistry (3rd Edition)
3rd Edition
ISBN: 9780321937711
Author: Paula Yurkanis Bruice
Publisher: PEARSON
expand_more
expand_more
format_list_bulleted
Concept explainers
Question
Chapter 17.3, Problem 4P
Interpretation Introduction
Interpretation:
Reason for the carboxylic group of the amino acid is more acidic than a carboxylic acid of acetic acid has to be given.
Concept Introduction:
Acid-base properties of Amino acids:
Every amino acid has a carbonyl group and an amino group, and each group can exist in an acidic form or a basic form, depending on
The compound exists primarily in the acidic form in solutions that are more acidic than their
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solutionStudents have asked these similar questions
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?
A naturally occurring amino acid such as alanine has a group that is a carboxylic acid and a group that is a protonated amine. a. If the pKa value of a carboxylic acid such as acetic acid is about 5 (see Table 2.1), then why is the pKa value of the carboxylic acid group of alanine so much lower? b. Draw the structure of alanine in a solution at pH = 0. c. Draw the structure of alanine in a solution at physiological pH (pH 7.4). d. Draw the structure of alanine in a solution at pH = 12. e. Is there a pH at which alanine is uncharged (that is, neither group has a charge)? f. At what pH does alanine have no net charge (that is, the amount of negative charge is the same as the amount of positive charge)?
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
Chapter 17 Solutions
Essential Organic Chemistry (3rd Edition)
Ch. 17.1 - a. Explain why, when the imidazole ring of...Ch. 17.2 - Prob. 2PCh. 17.3 - Prob. 3PCh. 17.3 - Prob. 4PCh. 17.3 - Prob. 6PCh. 17.4 - Calculate the pI of each of the following amino...Ch. 17.4 - a. Which amino acid has the lowest pI value? b....Ch. 17.5 - What aldehyde is formed when valine is treated...Ch. 17.5 - Prob. 10PCh. 17.5 - Prob. 11P
Ch. 17.5 - Prob. 12PCh. 17.6 - Prob. 13PCh. 17.6 - What amino acid would be formed using the...Ch. 17.6 - What amino acid would be formed when the aldehyde...Ch. 17.7 - Pig liver esterase is an enzyme that catalyzes the...Ch. 17.8 - Prob. 17PCh. 17.8 - Prob. 18PCh. 17.8 - Prob. 19PCh. 17.8 - Prob. 20PCh. 17.10 - Prob. 21PCh. 17.10 - Prob. 22PCh. 17.10 - Why does cyanogen bromide not cleave on the C-side...Ch. 17.10 - Prob. 24PCh. 17.10 - Prob. 26PCh. 17.12 - Prob. 27PCh. 17.13 - a. Which would have the greatest percentage of...Ch. 17 - Draw the predominant form of the following amino...Ch. 17 - What is the pI of serine?Ch. 17 - Prob. 31PCh. 17 - Prob. 32PCh. 17 - Which would have a higher percentage of negative...Ch. 17 - Draw the form of aspartate that predominates at...Ch. 17 - Prob. 35PCh. 17 - A professor was preparing a manuscript for...Ch. 17 - a. Why is the pKa of the glutamate side chain...Ch. 17 - Prob. 38PCh. 17 - Determine the amino acid sequence of a polypeptide...Ch. 17 - Prob. 40PCh. 17 - Prob. 41PCh. 17 - Three peptides were obtained from a trypsin...Ch. 17 - Prob. 43PCh. 17 - After the polypeptide shown here was treated with...Ch. 17 - The disulfide bridges of a polypeptide were...Ch. 17 - -Amino acids can be prepared by treating an...Ch. 17 - Reaction of a polypeptide with carboxypeptidase A...Ch. 17 - Prob. 48PCh. 17 - Prob. 49PCh. 17 - Show how valine can be prepared by a. a Strecker...Ch. 17 - Prob. 51PCh. 17 - Why is proline never found in an -helix?Ch. 17 - Determine the amino acid sequence of a polypeptide...Ch. 17 - Prob. 55PCh. 17 - A chemist wanted to test his hypothesis that the...Ch. 17 - A normal polypeptide and a mutant of the...
Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, chemistry and related others by exploring similar questions and additional content below.Similar questions
- The pKa values for the amino and carboxyl groups of alanine are 9.69 and 2.35, respectively. Calculate the pH of 10 mL of 50 mM alanine buffer (pH 10) following the addition of: a. 0.1 mL of 1.5 M HCl b. 0.3 mL of 1.5 M HClarrow_forward(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?arrow_forwardConsider the amino acid and its pKa values:Lysine: pKa1= 2.18 pKa2= 8.95, pKaR=10.79 a. Calculate the isoelectric point.b. What will be the net charge on lysine at the isoelectric point?c. In what direction will the lysine move when placed in an electric field at a pH value of 6.68d. Which form of the lysine is the least soluble in water?e. Draw the structure of the lysine which is the least soluble in water?arrow_forward
- Arginine is an amino acid which has the following pKa values: pK1: 2.17, pK2: = 9.04, pKR = 12.48. Calculate the net charge of arginine at the pH value of 4.arrow_forwardExplain why the pI of lysine is the average of the pKa values of its two protonated amino groups.arrow_forwardExplain why the pKa of the - NH3+ group of an a-amino acid is lower than the pKa of the ammonium ion derived from a 1° amine (RNH3+). For example the pKa of the - NH3+ group of alanine is 9.87 but the pKa of CH3NH3+ is 10.63.arrow_forward
- Why is the pK of the carboxyl group of glycine (pK = 2.3) less than that for acetic acid (pK = 4.76)?arrow_forwardThe pKa values of each group are shown above. In the structures below, fill in the missing atoms/charges for the amino acid at each indicated pH.arrow_forwardAlanine has pKa values of 2.34 and 9.69. Therefore, alanine exists predominately as a zwitterion in anaqueous solution with pH 7 ____ and pH 6 ____.arrow_forward
- 5. Which amino acid listed in the pKa table may behave as a zwitterion at a pH of 7.0-7.4?arrow_forwardExplain why the pKa of the ‒ NH3+ group of an α-amino acid is lower than the pKa of the ammonium ion derived from a 1° amine (RNH3+). For example the pKa of the ‒ NH3+ group of alanine is 9.87 but the pKa of CH3NH3+ is 10.63.arrow_forwardThe side chain of acetyl-L-lysine-OMe has a pKa=10.5 and its acid-dissociation reaction is shown below. C. what is the pH of a solution wherein the ration of [A-]/[HA]=1:10?arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
- Introduction to General, Organic and BiochemistryChemistryISBN:9781285869759Author:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar TorresPublisher:Cengage Learning
Introduction to General, Organic and Biochemistry
Chemistry
ISBN:9781285869759
Author:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres
Publisher:Cengage Learning