EBK ORGANIC CHEMISTRY
8th Edition
ISBN: 8220102744127
Author: Bruice
Publisher: PEARSON
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Chapter 21, Problem 51P
A titration curve is a plot of the pH of a solution as a function of added equivalents of hydroxide ion. As hydroxide ion is added to the aqueous solution, the pH increases because hydroxide ion removes protons from the solution. The pH flattens out when hydroxide ion can remove a proton from an ionziable group of an amino acid rather than a proton from the solution. Identify the amino acids that give the titration curves below.
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Chapter 21 Solutions
EBK ORGANIC CHEMISTRY
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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- (a) Draw the Lewis structure for the amino acid phenylalanine, showing the amino group and the carboxylic group in their un-ionized forms. (b) Draw the Lewis structure for the zwitterionic form of phenylalanine. (c) Which of these structures will be the predominant form at physiological pH?arrow_forwardat a pH value of 2, the amino and carboxyl groups in an amino acid will exist asarrow_forwardWhen a weak monoprotic acid (HA) is titrated with NaOH, which of the following forms of the acid is present at buffering region? In the titration of a weak acid with an unknown solution with NaOH, which of the following goes into the burette? An amino acid can be considered as a polyprotic acid, true or false?arrow_forward
- please explain why this happends, im having trouble in this section. Part A Chymotrypsin, an enzyme that hydrolyzes peptide bonds in proteins, functions in the small intestine at an optimum pH of 7.7 to 8.0. How is the rate of the chymotrypsin-catalyzed reaction affected by each of the following conditions?arrow_forwardWhat effect did high and low temperatures have on enzyme activity? Why?arrow_forward. Describe the pH range of acceptable buffering behavior for the amino acids alanine, histidine, aspartic acid, and lysine.arrow_forward
- The first step in the procedure asks you to prepare five dilutions of the protein standard (BSA) in the range of 0.2 to 1.0 mg/ml. For each concentration, a volume of 1.0 mL should be prepared. Describe how you will prepare these standards using a stock solution of BSA that is 2.0 mg/ml.arrow_forwardA student added a total of 75 mL sodium hydroxide to titrate an amino acid solution of unknown concentration. They also calculated that they added a total of 14 mL of sodium hydroxide to arrive at pH 2.6 and a total of 32 mL of sodium hydroxide to arrvive at pH 4.8. Information about the molarity of the sodium hydroxide solution used and the initial volume of the unknown amino acid can be derived from the image. What was the initial concentration of the amino acid solution in milimolar (mM)? The calculations must be presented such that those can be recapitulated by the marker. Provide the answer with no decimal places. Show all details of your working out. State the answer in a full sentencearrow_forwardPlease send me the question in 20 minutes it's very urgent plzarrow_forward
- The amino acid glycine is often used as the main ingredient of a buffer in biochemical experiments. The amino group of glycine, which has a pk of 9.6, can exist either in the protonated form -NH or as the free base -NH₂, because of the reversible equilibrium R-NH² ⇒ R-NH₂ + H* In what pH range can glycine be used as an effective buffer due to its amino group? How much 5 M KOH must be added to 1.0 L of 0.1 M glycine at pH 9.0 to bring its pH to 10.0? In a 0.1 M solution of glycine at pH 9.0, what fraction of glycine has its amino group in the -NH; form? When 99% of the glycine is in its -NH, form, what is the numerical relation between the pH of the solution and the pK, of the amino group? Aarrow_forwardAll amino acids have two ionizable functional groups: an α‑amino group (average p?a of 9.4) and an α‑carboxylic acid group (average p?a of 2.2). Aspartic acid has an ionizable side chain (R group) with a p?a of about 3.8. One of the possible ionization states of aspartic acid is shown in the image. The protonated form of the R group of aspartic acid is shown in the structure. The ratio of the protonated form to the charged (deprotonated) form depends on the p?a of the R group and the pH of the solution. Select all the pH values at which the charged form of the R group would predominate.arrow_forwardDraw a titration curve for the amino acid lysine at the pKa's of 2.2, 9.0, and 10.0 for the ionizable groups of lysine. Label the buffering regions and equivalence points. Draw the structures for the primary species of lysine at all the buffering regions and equivalence points you include in your graph.arrow_forward
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