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…

Organic Chemistry

8th Edition

ISBN:9781305580350

Author:William H. Brown, Brent L. Iverson, Eric Anslyn, Christopher S. Foote

Publisher:William H. Brown, Brent L. Iverson, Eric Anslyn, Christopher S. Foote

Chapter25: Carbohydrates

Section: Chapter Questions

Problem 25.48P

See similar textbooks

Similar questions

1. How many amino sugars can you see? 2. What pharmacophore is present in the structure?
Glycosaminoglycans (GAGs) are heteropolysaccharides composed of repeating disaccharide units. These units have some similar characteristics that allow them to be identified as GAGS. Which of the structures are examples of glycosaminoglycans? А. C. E. HO HO COO™ H Н ОН Н CH₂OH H H H OH OH Н CH₂OH Н OH H ОН o,so H H Н CH₂OH H H ОН H CH₂OSO H NH C=0 CH, H H Н NH c=0 CH3 H CH,OH OH Н ОН OH H B. D. Н НО H ОН H CH₂OH H ОН Н СОО ОН Н Н H H OSoz H Н OH б H CH₂OH ОН CH₂OSO H ОН H Н OSO, H Н NHSO,
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.
Explain the solubility behavior of each compound in water with relevance to their STRUCTURE. c. Amino Acids and Proteins in Water-Alanine (clear colorless solution)-Glutamic acid (clear colorless solution)-Arginine (clear colorless solution)-Albumin (clear colorless solution)-Casein (clear colorless solution)
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
Determine whether each of the following aqueous solutions are likely to be optically active or inactive. a. a solution of ethanol, CH3CH2OHb. a solution of (+)-Alaninec. a solution containing equimolar quantities of (+)-Alanine and (–)-Alanine
Which R group would most likely be found in a hydrophobic area of the tertiary structure of a globular protein? * A. -CH3 В. -СH,ОН C. -CH,COO- D. -SH Е. -СH, CONH,
Please answer item number 3 only.
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 treated a sample of an enzyme that contained four disulfide bridges with 2-mercaptoethanol 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?
Please don't provide handwritten solution ..... Does tyrosine contain p-pi or pi-pi conjugation?
The shown image is a reaction diagram for the hydrolysis of peptide bonds. Appropriately substituted phosphonates (structure shown above) were successfully designed as strong inhibitors for proteolytic enzymes. Explain why this strategy was successful. Note that the lengths of P–O bonds in phosphonates are significantly longer than the corresponding C–O bonds.
NOT a graded assignment. From my understanding it is just (Delta G) = (Delta H) - (T)(Delta S) for part A. I am confused about the "unfolding" part and the last part.

SEE MORE QUESTIONS

Recommended textbooks for you

Organic Chemistry

Chemistry

ISBN:

9781305580350

Author:

William H. Brown, Brent L. Iverson, Eric Anslyn, Christopher S. Foote

Publisher:

Cengage Learning

Organic Chemistry: A Guided Inquiry

Chemistry

ISBN:

9780618974122

Author:

Andrei Straumanis

Publisher:

Cengage Learning

Chemistry & Chemical Reactivity

Chemistry

ISBN:

9781337399074

Author:

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

Publisher:

Cengage Learning

Organic Chemistry

Chemistry

ISBN:

9781305580350

Author:

William H. Brown, Brent L. Iverson, Eric Anslyn, Christopher S. Foote

Publisher:

Cengage Learning

Organic Chemistry: A Guided Inquiry

Chemistry

ISBN:

9780618974122

Author:

Andrei Straumanis

Publisher:

Cengage Learning

Chemistry & Chemical Reactivity

Chemistry

ISBN:

9781337399074

Author:

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

Publisher:

Cengage Learning

Chemistry & Chemical Reactivity

Chemistry

ISBN:

9781133949640

Author:

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

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

Chemistry: Principles and Reactions

Chemistry

ISBN:

9781305079373

Author:

William L. Masterton, Cecile N. Hurley

Publisher:

Cengage Learning

SEE MORE TEXTBOOKS