Organic Chemistry, Books a la Carte Edition (8th Edition)
8th Edition
ISBN: 9780134074580
Author: Bruice, Paula Yurkanis
Publisher: PEARSON
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Textbook Question
Chapter 21, Problem 53P
Aspartame (its structure is on page 1007) has a pl of 5.9. Draw its prevailing form at physiological pH (7.4).
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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
Aspartame has a pI of 5.9. Draw its prevailing form at physiological pH (7.4).
An optically inactive triglyceride V (MW = 680) yielded one mole of myristic acid (14:0)
and two moles of myristoleic acid (14:1).
Draw the structure of the triglyceride V.
Calculate the iodine number of triglyceride V.
Draw the product(s) when triglyceride V reacts H2/Ni.
i.
ii.
111.
(Relative atomic mass: C=12, H=1, 0=16, I=127)
Chapter 21 Solutions
Organic Chemistry, Books a la Carte Edition (8th Edition)
Ch. 21.1 - a. Explain why, when the imidazole ring of...Ch. 21.2 - a. Which isomer(R)-alanine or (S)-alanineis...Ch. 21.2 - Prob. 4PCh. 21.3 - Prob. 5PCh. 21.3 - Prob. 6PCh. 21.3 - Draw the predominant form for glutamate in a...Ch. 21.3 - a. Why is the pKa of the glutamate side chain...Ch. 21.4 - Calculate the pI of each of the following amino...Ch. 21.4 - a. Which amino acid has the lowest pI value? b....Ch. 21.4 - Prob. 12P
Ch. 21.4 - Prob. 13PCh. 21.4 - Explain why the pI of lysine is the average of the...Ch. 21.5 - What aldehyde is formed when valine is treated...Ch. 21.5 - Prob. 16PCh. 21.5 - Prob. 17PCh. 21.5 - Prob. 18PCh. 21.5 - Prob. 19PCh. 21.6 - Why is excess ammonia used in the preceding...Ch. 21.6 - Prob. 21PCh. 21.6 - What amino acid is formed using the...Ch. 21.6 - Prob. 23PCh. 21.6 - What amino acid is formed when the aldehyde used...Ch. 21.7 - Esterase is an enzyme that catalyzes the...Ch. 21.8 - Draw the tetrapeptide Ala-Thr-Asp-Asn and indicate...Ch. 21.8 - Draw the resonance contributors of the peptide...Ch. 21.8 - Which bonds in the backbone of a peptide can...Ch. 21.9 - An opioid pentapeptide has the following...Ch. 21.9 - What is the configuration about each of the...Ch. 21.9 - Glutathione is a tripeptide whose function is to...Ch. 21.10 - What dipeptides would be formed by heating a...Ch. 21.10 - Suppose you are trying to synthesize the dipeptide...Ch. 21.10 - Show the steps in the synthesis of the...Ch. 21.10 - a. Calculate the overall yield of bradykinin when...Ch. 21.11 - Show the steps in the synthesis of the...Ch. 21.13 - Prob. 37PCh. 21.13 - In determining the primary structure of insulin,...Ch. 21.13 - A decapeptide undergoes partial hydrolysis to give...Ch. 21.13 - Explain why cyanogen bromide does not cleave on...Ch. 21.13 - Indicate the peptides produced from cleavage by...Ch. 21.14 - Prob. 43PCh. 21.14 - Three peptides were obtained from a trypsin...Ch. 21.14 - Prob. 45PCh. 21.15 - How would a protein that resides in the nonpolar...Ch. 21.16 - a. Which would have the greatest percentage of...Ch. 21.17 - When apples that have been cut are exposed to...Ch. 21 - Glycine has pK2 values of 2.34 and 9.60. At what...Ch. 21 - Prob. 50PCh. 21 - A titration curve is a plot of the pH of a...Ch. 21 - Prob. 52PCh. 21 - Aspartame (its structure is on page 1007) has a pl...Ch. 21 - Draw the form of aspartate that predominates at...Ch. 21 - Show how phenylalanine can be prepared by...Ch. 21 - A professor was preparing a manuscript for...Ch. 21 - What aldehydes are formed when the following amino...Ch. 21 - Prob. 58PCh. 21 - Determine the amino acid sequence of a polypeptide...Ch. 21 - Prob. 60PCh. 21 - Prob. 61PCh. 21 - Which is the more effective buffer at...Ch. 21 - Identify the location and type of charge on the...Ch. 21 - Draw the product obtained when a lysine side chain...Ch. 21 - After the polypeptide shown below was treated with...Ch. 21 - Treatment of a polypeptide with 2-mercaptoethanol...Ch. 21 - Show how aspartame can be synthesized using DCCD.Ch. 21 - -Amino acids can be prepared by treating an...Ch. 21 - Reaction of a polypeptide with carboxypeptidase A...Ch. 21 - a. How many different octapeptides can be made...Ch. 21 - Glycine has pKa values of 2.3 and 9.6. Do you...Ch. 21 - A mixture of 15 amino acids gave the fingerprint...Ch. 21 - Write the mechanism for the reaction of an amino...Ch. 21 - Prob. 74PCh. 21 - Show how valine can be prepared by a. a...Ch. 21 - The primary structure of -endorphin, a peptide...Ch. 21 - A chemist wanted to test his hypothesis that the...Ch. 21 - Propose a mechanism for the rearrangement of the...Ch. 21 - A normal polypeptide and a mutant of the...Ch. 21 - Determine the amino acid sequence of a polypeptide...
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- 1. If the pl for asparagine is 5.43, draw the structure at a pH of 9.5?arrow_forward25) Valine is one of the essential amino acids found in our bodies and used in the production of proteins. Valine has the condensed formula (CH3)2CH(NH2)CHCO2H. Draw the skeletal structure of valine as it would be represented at physiological pH (7.4). Answer:arrow_forwardDraw the predominant form the histidine amino acids at physiological pH (7.4):arrow_forward
- 4a) Canavanine is an amino acid that is produced by some legume plants. It is not used in proteins but serves as a nitrogen storage molecule in seeds, and is being investigated as a possible anti-cancer and anti-viral drug. Canavanine's amino and carboxyl groups are the same as those in any other amino acid (pKa for the amino group is 8.0 and pKa for the carboxyl group is 3.1), and its side group has a single ionizable group with a pKa of 7.0. Describe or explain what that statement (the previous sentence) tells you about the protonation state of each of the 3 ionizable groups on this amino acid if it is dissolved in pure distilled water at pH 7.0.arrow_forwardWhich functional group on furosemide’s structure below is most likely to be negatively charged at physiological pH (7.4)?arrow_forward11. (8) Draw the structure of the tripeptide: Asp-Cys-Lys in a solution with a pH of 6.0. What is the overall charge? Overall Charge=arrow_forward
- (Q25) A buffer solution is prepared by adding 0.797 moles of formic acid and 0.866 moles of sodium formate. What will the solution pH be if 0.228 moles of sodium hydroxide (NaOH) is added to the buffer solution? The Ką of formic acid is 1.8 x 104.arrow_forwardConsider the following peptide : Phe – Glu – Ser – Met and Val – Trp – Cys – Leu. Do these peptides have different net charges at (a) pH 1? (b) pH 7? Indicate the charges at both pH valuesarrow_forward3a) Consider a tripeptide (a peptide that's only 3 amino acidslong) composed of one molecule each of lysine, leucine, and thehypothetical amino acid lupine (which doesn't actually exist, sodon't try to look it up). Lupine has an ionizable side group with apa of 6.3. When this tripeptide is dissolved in an aqueoussolution at pH 5.0, the net charge on the molecule is +2. Givethe charge on the protonated form of the lupine side group, andthe charge on the deprotonated form of the lupine side group.show your work or explain how you determinedthe charge on each form of the lupine side groupsarrow_forward
- Draw the predominant form the lysine amino acids at physiological pH (7.4):arrow_forwardh) Specify the absolute (R/S) configuration of the amino group in structure IV. (i) If the substituents in structures I, IV and V were identical (all OH or all NH2), which structure would result in a meso compound? (j) If each hydroxy group for structures I, II and VI were replaced with another amino group, which compound would be made optically inactive?arrow_forwardQuestion 6 of 25 > Modify lysine to show the predominant form at pH 7. Modify the amino acid by adding or removing atoms or bonds and by adding charges where appropriate. Select Draw Rings More N 0 H / || III C H-O || C ▬▬▬▬▬▬▬▬▬▬▬▬▬▬▬▬▬▬▬▬▬▬▬▬▬▬▬ H H I C *一£一£一£一£ H H I N-H Erase Q2 Qarrow_forward
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