Essential Organic Chemistry (3rd Edition)
3rd Edition
ISBN: 9780321937711
Author: Paula Yurkanis Bruice
Publisher: PEARSON
expand_more
expand_more
format_list_bulleted
Concept explainers
Textbook Question
Chapter 17, Problem 56P
A chemist wanted to test his hypothesis that the disulfide bridges that form in many proteins do so after the minimum energy conformation of the protein has been achieved. He reduced a sample of an enzyme that contained four disulfide bridges and then added urea to denature the enzyme. He slowly removed these reagents so that the enzyme could re-fold and re-form the disulfide bridges. The enzyme he recovered had 80% of its original activity. What would be the percent activity in the recovered enzyme if disulfide bridge formation were entirely random rather than determined by the tertiary structure? Does this experiment support his hypothesis?
Expert Solution & Answer
Trending nowThis is a popular solution!
Students have asked these similar questions
(c) The following data have been obtained for the hydrolysis of sucrose, C12H22O11, to
glucose, C6H12O6, and fructose C6H12O6, in acidic solution:
C12H22O11 + H2O → C6H12O6 + C6H12O6
[sucrose]/mol dm³
t/min
0
0.316
14
0.300
39
0.274
60
0.256
80
0.238
110
0.211
(i) Graphically prove the order of the reaction and determine the rate constant of the
reaction.
(ii) Determine the half-life, t½ for the hydrolysis of sucrose.
(III) adsorbent
(b) Adsorption of the hexacyanoferrate (III) ion, [Fe(CN)6] ³, on y-Al2O3 from aqueous
solution was examined. The adsorption was modelled using a modified Langmuir
isotherm, yielding the following values of Kat pH = 6.5:
(ii)
T/K
10-10 K
280
2.505
295
1.819
310
1.364
325
1.050
Determine the enthalpy of adsorption, AadsHⓇ.
If the reported value of entropy of adsorption, Aads Se = 146 J K-1 mol-1 under the above
conditions, determine Aads Gº.
with full details solution please
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
- Zeroth Order Reaction In a certain experiment the decomposition of hydrogen iodide on finely divided gold is zeroth order with respect to HI. 2HI(g) Au H2(g) + 12(9) Rate = -d[HI]/dt k = 2.00x104 mol L-1 s-1 If the experiment has an initial HI concentration of 0.460 mol/L, what is the concentration of HI after 28.0 minutes? 1 pts Submit Answer Tries 0/5 How long will it take for all of the HI to decompose? 1 pts Submit Answer Tries 0/5 What is the rate of formation of H2 16.0 minutes after the reaction is initiated? 1 pts Submit Answer Tries 0/5arrow_forwardangelarodriguezmunoz149@gmail.com Hi i need help with this question i am not sure what the right answers are.arrow_forwardPlease correct answer and don't used hand raitingarrow_forward
- Don't used hand raitingarrow_forwardDon't used Ai solutionarrow_forwardSaved v Question: I've done both of the graphs and generated an equation from excel, I just need help explaining A-B. Below is just the information I used to get the graphs obtain the graph please help. Prepare two graphs, the first with the percent transmission on the vertical axis and concentration on the horizontal axis and the second with absorption on the vertical axis and concentration on the horizontal axis. Solution # Unknown Concentration (mol/L) Transmittance Absorption 9.88x101 635 0.17 1.98x101 47% 0.33 2.95x101 31% 0.51 3.95x10 21% 0.68 4.94x10 14% 24% 0.85 0.62 A.) Give an equation that relates either the % transmission or the absorption to the concentration. Explain how you arrived at your equation. B.) What is the relationship between the percent transmission and the absorption? C.) Determine the concentration of the ironlll) salicylate in the unknown directly from the graph and from the best fit trend-line (least squares analysis) of the graph that yielded a straight…arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
- World of Chemistry, 3rd editionChemistryISBN:9781133109655Author:Steven S. Zumdahl, Susan L. Zumdahl, Donald J. DeCostePublisher:Brooks / Cole / Cengage LearningWorld of ChemistryChemistryISBN:9780618562763Author:Steven S. ZumdahlPublisher:Houghton Mifflin College DivChemistry for Today: General, Organic, and Bioche...ChemistryISBN:9781305960060Author:Spencer L. Seager, Michael R. Slabaugh, Maren S. HansenPublisher:Cengage Learning
- Introductory Chemistry: An Active Learning Approa...ChemistryISBN:9781305079250Author:Mark S. Cracolice, Ed PetersPublisher:Cengage LearningIntroductory Chemistry: A FoundationChemistryISBN:9781337399425Author:Steven S. Zumdahl, Donald J. DeCostePublisher:Cengage LearningIntroduction to General, Organic and BiochemistryChemistryISBN:9781285869759Author:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar TorresPublisher:Cengage Learning
World of Chemistry, 3rd edition
Chemistry
ISBN:9781133109655
Author:Steven S. Zumdahl, Susan L. Zumdahl, Donald J. DeCoste
Publisher:Brooks / Cole / Cengage Learning
World of Chemistry
Chemistry
ISBN:9780618562763
Author:Steven S. Zumdahl
Publisher:Houghton Mifflin College Div
Chemistry for Today: General, Organic, and Bioche...
Chemistry
ISBN:9781305960060
Author:Spencer L. Seager, Michael R. Slabaugh, Maren S. Hansen
Publisher:Cengage Learning
Introductory Chemistry: An Active Learning Approa...
Chemistry
ISBN:9781305079250
Author:Mark S. Cracolice, Ed Peters
Publisher:Cengage Learning
Introductory Chemistry: A Foundation
Chemistry
ISBN:9781337399425
Author:Steven S. Zumdahl, Donald J. DeCoste
Publisher: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
Biomolecules - Protein - Amino acids; Author: Tutorials Point (India) Ltd.;https://www.youtube.com/watch?v=ySNVPDHJ0ek;License: Standard YouTube License, CC-BY