3. Properties of Isomers(a)Consider the following illustration of a protein binding pocket and two enantiomers.Assuming the most stabilizing interaction is an ionic bond between the ammonium (NH3+)and the carboxylate (CO₂¯), circle the enantiomer that has higher affinity for (i.e., bindsmore strongly to) the protein?(b).OH+H3N.HOHOenantiomer Aenantiomer Bhypothetical protein binding pocket= generic bulky group1) Compounds A and B undergo a reaction with an acid chloride to give compoundsC and D as shown below. Complete the table, indicating by writing "yes" or "no" whetherSiO2 chromatography and chiral chromatography can be used to separate compounds Aand B, and compounds B and D.H3CO CF3.CIH3CO CF3H3CO CF3OHOHCH3!!! CH 3base, solventCH3ABMoleculesAH3CO CF3CH3OH..OHSeparable by SiO2chromatography(yes or no)Separable by chiralchromatography(yes or no)CH3!!!!!CH 3BH3CO CF3Ο"""CH3C

Question (a)Enantiomer B: The carboxylate group (-COO⁻) is spatially oriented to form a better ionic…

Answered: 3. Properties of Isomers (a) Consider…

Chemistry & Chemical Reactivity

10th Edition

ISBN:9781337399074

Author:John C. Kotz, Paul M. Treichel, John Townsend, David Treichel

Publisher:John C. Kotz, Paul M. Treichel, John Townsend, David Treichel

Chapter24: Biochemistry

Section: Chapter Questions

Problem 4PS

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The amino acid alanine has the condensed structural formula CH3CH(NH2)CO2H. Which Fischer projection represents (R)-alanine? NH2 А. -CO2H CH3 NH2 H3C- ČO,H C. CO,H H3C- -NH2 H - D. CO,H to -NH2 CH3 B.
7. Explain why 2-phenylethyl boronic acid (Compound A) is an inhibitor of chymotrypsin, which is an enzyme that catalyzes the hydrolysis of peptide linkages. What type of inhibition do you think is exemplified here? OH -CH2-CH2 B HO, Compound A
Am I correct? Please help
(b) What is Ka of the 2-hydroxyethylammonium ion, HOCH2CH2NH3+ (pKb of HOCH2CH2CH2NH2 = 4.49)?
The chemical structure of cysteine (C3H-NO₂S) is shown below. Highlight each atom that is in an amino group. :S H | HC-H H-C | H-N-H :0: || C. -0-H X 5 Save For Late
© Macmillan Learning Match each structure and description to the appropriate amino acid. Glycine Histidine NH₁₂+ NH₁₂+ H HH III H-C-C-C-C-COO- H H CH, H no chiral centers ↓ H-C-COO H one chiral center 0 Resources Solution ? Hint Sub Penalized Isoleucine H NH₁* ↓ H-C=C-C-C-COO IIII ┃┃ -z' N H NH H H smallest R group R group partially protonated at physiological pH two chiral centers Answer Bank
Refer to the bar graph below, Explain why the n→π* interactions contributes more to the overall stabilization of the protein than all the other interactions(C-H-O hydrogen bond,π-π interactions, C5 Hydrogen Bonds, Cation-π interactions, Sulfur-arene interactions, Anion-π interactions, Chalcogen bonds, X-H-π interactions) even though n→π* is the weaker interaction. Explain why that's the case for EACH of the bonds. I.e Why n→π* interactions contribute more to the overall stabilization of the protein than C-H-O hydrogen bonds, even though n→π* is the weaker interaction. Why n→π* interactions contribute more to the overall stabilization of the protein than π-π interactions even though n→π* is the weaker interaction. Why n→π* interactions contribute more to the overall stabilization of the protein than C5 Hydrogen Bonds, even though n→π* is the weaker interaction. Why n→π* interactions contribute more to the overall stabilization of the protein than Cation-π interactions, even though…
Refer to the bar graph below, Explain why the n→π* interactions contributes more to the overall stabilization of the protein than all the other interactions(C-H-O hydrogen bond,π-π interactions, C5 Hydrogen Bonds, Cation-π interactions, Sulfur-arene interactions, Anion-π interactions, Chalcogen bonds, X-H-π interactions) even though n→π* is the weaker interaction. Explain why that's the case for EACH of the bonds. I.e Why n→π* interactions contribute more to the overall stabilization of the protein than C-H-O hydrogen bonds, even though n→π* is the weaker interaction. Why n→π* interactions contribute more to the overall stabilization of the protein than π-π interactions even though n→π* is the weaker interaction. Why n→π* interactions contribute more to the overall stabilization of the protein than C5 Hydrogen Bonds, even though n→π* is the weaker interaction. Why n→π* interactions contribute more to the overall stabilization of the protein than Cation-π interactions, even though…
Candoxatrilat is a potent neutral endopeptidase (NEP) inhibitor. Researchers designed multiple prodrugs of Candoxatrilat and tested their efficiency. Based on their structure, which one do you think is more likely to be most fast-acting? అస్ రినంన నేంి OMe OMe OMe CO,H Compound A Compound B но, OMe OMe Candoxatrilat CH Co,H Compound C Compound D O C
8. The following proteins represent a wide range of molecular weights and isoelectric points. Mr is the molecular weight of a single protein chain. • Protein 1: Mr 68,544; pl 6.11 (monomer) • Protein 2: Mr 29,041; pl 5.32 (dimer) • Protein 3: Mr 15,805; pl 5.7 (dimer) • Protein 4: Mr 12,165; pl 4.74 a. Which protein is the most acidic? Explain your answer. b. Which protein will migrate the slowest in an SDS-PAGE? Explain your answer. c. In what order will these proteins elute from a cation exchanger at pH 8? Explain your answer. d. In what order will these proteins salt out from a pH 7 solution by the dropwise addition of saturated ammonium sulfate? Explain your answer. 5 83°F Cloudy
H. H. H. CH2 (CH2)4 NH3* CH2 но CH CH, CH CH2 CH2 H. (a) (b) (e) Which of the interactions stabilizing protein tertiary structure is (a)? O hydrophobic interaction O disulphide bridge bonding O hydrogen bonding O salt bridge bonding
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). Tyrosine also has an ionizable side chain (R group) with a pK, of about 10.1. One of the possible ionization states of tyrosine is shown. H3N-CH -C-OH CH2 ÓH At what pH would the structure be the predominant ionization state? Consider the ionization state of all three of the functional groups. The protonated form of the R group of tyrosine is shown in the structure. The ratio of the protonated form to the charged (deprotonated) form depends on the pK, of the R group and the pH of the solution. Select the pH value at which the charged form of the R group would predominate.

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