PKG ORGANIC CHEMISTRY
5th Edition
ISBN: 9781259963667
Author: SMITH
Publisher: MCG
expand_more
expand_more
format_list_bulleted
Question
Chapter 29, Problem 29.47P
Interpretation Introduction
Interpretation: The steps that show that resolution process of alanine are to be stated.
Concept introduction: The chemical compounds in which carbon atom is bonded to
Expert Solution & Answer
Trending nowThis is a popular solution!
Students have asked these similar questions
(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?
the pKa values for phenylalanine are 1.83 (carboxyl group) and 9.13 (amino group). Use the Henderson-hasselbach equation to determine the ratio of the acidic and basic forms of each of the ionizing groups of phenylalanine at neutral pH. Based on this, draw the predominant structure of phenylalanine at neutral pH.
Answer the following questions on the basis of the free energies of formation
at 25°C shown in the table at the top of the next page:
(a) Does the peptide bond between alanine and glycine form spontaneously
under standard conditions?
Chapter 29 Solutions
PKG ORGANIC CHEMISTRY
Ch. 29 - Prob. 29.1PCh. 29 - Problem 29.2
What form exists at the isoelectric...Ch. 29 - Problem 29.3
Explain why the of the group of an...Ch. 29 - Prob. 29.4PCh. 29 - Problem 29.5
What -halo carbonyl compound is...Ch. 29 - Problem 29.6
The enolate derived from diethyl...Ch. 29 - Problem 29.7
What amino acid is formed when is...Ch. 29 - Problem 29.8
What aldehyde is needed to synthesize...Ch. 29 - Problem 29.9
Draw the products of each...Ch. 29 - Prob. 29.10P
Ch. 29 - Prob. 29.11PCh. 29 - Prob. 29.12PCh. 29 - Problem 29.13
What alkene is needed to synthesize...Ch. 29 - Problem 29.14
Draw the structure of each peptide....Ch. 29 - Problem 29.15
Name each peptide using both the...Ch. 29 - Prob. 29.16PCh. 29 - Prob. 29.17PCh. 29 - Problem 29.18
Glutathione, a powerful antioxidant...Ch. 29 - Problem 29.19
Draw the structure of the...Ch. 29 - Problem 29.20
Give the amino acid sequence of an...Ch. 29 - a What products are formed when each peptide is...Ch. 29 - Prob. 29.22PCh. 29 - Devise a synthesis of each peptide from amino acid...Ch. 29 - Devise a synthesis of the following dipeptide from...Ch. 29 - Prob. 29.25PCh. 29 - Consider two molecules of a tetrapeptide composed...Ch. 29 - What types of stabilizing interactions exist...Ch. 29 - Prob. 29.28PCh. 29 - Draw the product formed when the following amino...Ch. 29 - With reference to the following peptide: a...Ch. 29 - Devise a synthesis of the following dipeptide from...Ch. 29 - Prob. 29.32PCh. 29 - Histidine is classified as a basic amino acid...Ch. 29 - Tryptophan is not classified as a basic amino acid...Ch. 29 - What is the structure of each amino acid at its...Ch. 29 - What is the predominant form of each of the...Ch. 29 - 29.37 What is the predominant form of each of the...Ch. 29 - a. Draw the structure of the tripeptide A–A–A, and...Ch. 29 - 29.39 Draw the organic products formed in each...Ch. 29 - 29.40 What alkyl halide is needed to synthesize...Ch. 29 - 29.41 Devise a synthesis of threonine from diethyl...Ch. 29 - 29.42 Devise a synthesis of each amino acid from...Ch. 29 - Prob. 29.43PCh. 29 - Prob. 29.44PCh. 29 - Prob. 29.45PCh. 29 - Prob. 29.46PCh. 29 - Prob. 29.47PCh. 29 - 29.48 Brucine is a poisonous alkaloid obtained...Ch. 29 - Prob. 29.49PCh. 29 - Prob. 29.50PCh. 29 - Draw the structure for each peptide: (a) Phe–Ala;...Ch. 29 - 29.52 For the tetrapeptide Asp–Arg–Val–Tyr:
a....Ch. 29 - Prob. 29.53PCh. 29 - Prob. 29.54PCh. 29 - 29.55 Draw the amino acids and peptide fragments...Ch. 29 - Prob. 29.56PCh. 29 - Prob. 29.57PCh. 29 - Prob. 29.58PCh. 29 - 29.59 An octapeptide contains the following amino...Ch. 29 - 29.60 Draw the organic products formed in each...Ch. 29 - Draw all the steps in the synthesis of each...Ch. 29 - 29.62 Write out the steps for the synthesis of...Ch. 29 - 29.63 Besides the Boc and Fmoc protecting groups...Ch. 29 - 29.64 Another method to form a peptide bond...Ch. 29 - 29.65 Draw the mechanism for the reaction that...Ch. 29 - 29.66 Which of the following amino acids are...Ch. 29 - 29.67 After the peptide chain of collagen has been...Ch. 29 - Prob. 29.68PCh. 29 - Prob. 29.69PCh. 29 - 29.70 The anti-obesity drug orlistat works by...Ch. 29 - Prob. 29.71P
Knowledge Booster
Similar questions
- Ethyleneimine reacts with cysteine side chains in proteins to form S - aminoethyl derivatives. The peptide bonds on the carboxyl side of these modified cysteine residues are susceptible to hydrolysis by trypsin . Why?arrow_forwardThere are 20 common, naturally occurring amino acids from which all proteins are derived (as will be discussed in Chapter 25), although many other less common amino acids have been isolated from natural sources. Valine is one of the 20 common amino acids, and it was used as a starting material in the laboratory synthesis of an uncommon amino acid (Tetrahedron 1997, 53, 1151-1156). During one of the steps in the synthesis, compound 1 was treated with HBr under conditions that favor radical addition, giving stereoisomers 2 and 3. Draw the structures of 2 and 3, and describe their stereoisomeric relationship. H. LOCH3 HBr 2 + 3 hv H (S)-valine Modify the given copies of compound 1 to drawthe structures of 2 and 3. You can use the single bond tool to add/remove double bonds. CH2 CH2 H,C- H3C- -CH, -CH, Edit Drawing Describe the relationship of 2 and 3. O They are enantiomers. O They are superimposable. They are diastereomers. O They are constitutional isomers.arrow_forwardrefer to (Org. Lett. 2021, 23, 6278−6282).arrow_forward
- The side chain of cysteine is weakly acidic. Suppose in a protein, the side chain of a cysteine residue is surrounded by the side chains of several isoleucine residues. Would this make the side chain of the cysteine residue more acidic or less acidic? Please explain your answer.arrow_forwardExplain why the pI of lysine is the average of the pKa values of its two protonated amino groups.arrow_forwardThe BOC-protecting group may be added by treatment of an amino acid with di-tert- butyl dicarbonate as shown in the following reaction sequence. Propose a mechanism to account for formation of these products. (CH3),COCOČOC(CH3), + H2NCHCOO- (CH),COČNHCHCOO-+ (CH,),COH + CO, Di-tert-butyl dicarbonate BOC-amino acidarrow_forward
- G.293.arrow_forward. Describe the pH range of acceptable buffering behavior for the amino acids alanine, histidine, aspartic acid, and lysine.arrow_forwardA naturally occurring amino acid such as alanine has a group that is a carboxylic acid and a group that is a protonated amine. The pKa values of the two groups are shown.(a). If the pKa value of a carboxylic acid such as acetic acid is about 5, 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)?arrow_forward
- Glycine is a diprotic acid, which can potentially undergo two dissociation reactions, one for the a-amino group (-NH3), and the other for the carboxyl (-COOH) group. Therefore, it has two pKą values. The carboxyl group has a pK₁ of 2.34 and the a-amino group has a pK₂ of 9.60. Glycine can exist in fully deprotonated (NH₂-CH₂-COO-), fully protonated (NH3-CH₂-COOH), or zwitterionic form (NH3-CH₂-COO-). Match the pH values with the corresponding form of glycine that would be present in the highest concentration in a solution of th pH. fully deprotonated form NH,−CH,−COO- pH 11.9 pH 6.0 pH 8.0 fully protonated form NH3-CH₂-COOH pH 1.0 Answer Bank pH 7.0 zwitterionic form NH3-CH₂-COO-arrow_forwardThe pka of ascorbic acid is 4.2 at 24C. At what pH is the ratio of the deprotonated form to the protonated form 10:1? Prove using the Henderson-Hasselback equation. How to resolve this.arrow_forwardYou are going to be using Isoleucine in a buffer. The pKa of the carboxylate group of Isoleucine is 2.36 If you have a 0.1 M solution of Isoleucine at pH 3.22, what fraction (or percent) of the solution is in the deprotonated (COO- ) form?arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
Organic ChemistryChemistryISBN:9781305580350Author:William H. Brown, Brent L. Iverson, Eric Anslyn, Christopher S. FootePublisher:Cengage Learning
Chemistry: Principles and ReactionsChemistryISBN:9781305079373Author:William L. Masterton, Cecile N. HurleyPublisher:Cengage Learning
Organic Chemistry
Chemistry
ISBN:9781305580350
Author:William H. Brown, Brent L. Iverson, Eric Anslyn, Christopher S. Foote
Publisher:Cengage Learning
Chemistry: Principles and Reactions
Chemistry
ISBN:9781305079373
Author:William L. Masterton, Cecile N. Hurley
Publisher:Cengage Learning