Organic Chemistry & Study Guide and Student Solutions Manual for Organic Chemistry, Books a la Carte Edition (7th Edition)
7th Edition
ISBN: 9780321950123
Author: Paula Yurkanis Bruice
Publisher: PEARSON
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Chapter 22, Problem 50P
Interpretation Introduction
Interpretation:
The amino acid having greatest amount of negative charge at pH 7.4 has to be identified from amino acids leucine and asparagine.
Concept introduction:
The isoelectric point
The value of
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Valine has pKa's of 2.286 and 9.719. Estimate the fractional composition of Valine in the -1 form at pH=6.
A professor was preparing a manuscript for publication in which she reported that the pI of the tripeptide Lys-Lys-Lys was 10.6. One of her students pointed out that there must be an error in her calculations because the pKa of the e-amino group of lysine is 10.8 and the pI of the tripeptide has to be greater than any of its individual pKa values. Was the student correct?
His-Met-Asp-Tyr-Phe-Ser
Calculate an approximate pI (isoelectric point) for this peptide.
Chapter 22 Solutions
Organic Chemistry & Study Guide and Student Solutions Manual for Organic Chemistry, Books a la Carte Edition (7th Edition)
Ch. 22.1 - a. Explain why, when the imidazole ring of...Ch. 22.2 - a. Which isomer(R)-alanine or (S)-alanineis...Ch. 22.2 - Prob. 4PCh. 22.3 - Prob. 5PCh. 22.3 - Prob. 6PCh. 22.3 - Draw the predominant form for glutamate in a...Ch. 22.3 - a. Why is the pKa of the glutamate side chain...Ch. 22.4 - Explain why the pI of lysine is the average of the...Ch. 22.4 - Calculate the pI of each of the following amino...Ch. 22.4 - a. Which amino acid has the lowest pI value? b....
Ch. 22.4 - Prob. 13PCh. 22.5 - What aldehyde is formed when valine is treated...Ch. 22.5 - Prob. 15PCh. 22.5 - Prob. 16PCh. 22.5 - Prob. 17PCh. 22.5 - Prob. 18PCh. 22.6 - Why is excess ammonia used in the preceding...Ch. 22.6 - Prob. 20PCh. 22.6 - What amino acid is formed using the...Ch. 22.6 - Prob. 22PCh. 22.6 - What amino acid is formed when the aldehyde used...Ch. 22.7 - Esterase is an enzyme that catalyzes the...Ch. 22.8 - Draw the tetrapeptide Ala-Thr-Asp-Asn and indicate...Ch. 22.8 - Prob. 26PCh. 22.8 - Prob. 27PCh. 22.8 - Which bonds in the backbone of a peptide can...Ch. 22.9 - What is the configuration about each of the...Ch. 22.9 - Glutathione is a tripeptide whose function is to...Ch. 22.10 - What dipeptides would be formed by heating a...Ch. 22.10 - Suppose you are trying to synthesize the dipeptide...Ch. 22.10 - Show the steps in the synthesis of the...Ch. 22.10 - a. Calculate the overall yield of bradykinin when...Ch. 22.11 - Show the steps in the synthesis of the...Ch. 22.13 - Prob. 36PCh. 22.13 - In determining the primary structure of insulin,...Ch. 22.13 - A decapeptide undergoes partial hydrolysis to give...Ch. 22.13 - Explain why cyanogen bromide does not cleave on...Ch. 22.13 - Indicate the peptides produced from cleavage by...Ch. 22.13 - Prob. 42PCh. 22.13 - Three peptides were obtained from a trypsin...Ch. 22.14 - Prob. 44PCh. 22.15 - How would a protein that resides in the nonpolar...Ch. 22.16 - a. Which would have the greatest percentage of...Ch. 22 - Prob. 47PCh. 22 - Glycine has pK2 values of 2.34 and 9.60. At what...Ch. 22 - Prob. 49PCh. 22 - Prob. 50PCh. 22 - Aspartame (its structure is on page 1007) has a pl...Ch. 22 - Draw the form of aspartate that predominates at...Ch. 22 - A professor was preparing a manuscript for...Ch. 22 - Prob. 54PCh. 22 - Determine the amino acid sequence of a polypeptide...Ch. 22 - Prob. 56PCh. 22 - Which is the more effective buffer at...Ch. 22 - Identify the location and type of charge on the...Ch. 22 - Draw the product obtained when a lysine side chain...Ch. 22 - After the polypeptide shown below was treated with...Ch. 22 - Treatment of a polypeptide with 2-mercaptoethanol...Ch. 22 - Show how aspartame can be synthesized using DCCD.Ch. 22 - -Amino acids can be prepared by treating an...Ch. 22 - Reaction of a polypeptide with carboxypeptidase A...Ch. 22 - a. How many different octapeptides can be made...Ch. 22 - Glycine has pKa values of 2.3 and 9.6. Do you...Ch. 22 - A mixture of 15 amino acids gave the fingerprint...Ch. 22 - Write the mechanism for the reaction of an amino...Ch. 22 - Prob. 69PCh. 22 - Show how valine can be prepared by a. a...Ch. 22 - A chemist wanted to test his hypothesis that the...Ch. 22 - Propose a mechanism for the rearrangement of the...Ch. 22 - A normal polypeptide and a mutant of the...Ch. 22 - Determine the amino acid sequence of a polypeptide...
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- 3. A homopolymer of histidine (polyhistidine) adopts an alpha helix structure at pH 9 but is unfolded at a pH of 4. Explain why using chemical details.arrow_forwardEstimate the charge of the following oligopeptides at pH 7 based on the pKa values of the constituent amino acids! Ser-His-Ala-Gly-Lys-Asparrow_forwardThe pKa value for adenine (N-1) is 4.2. Using the Henderson-Hasselbalch equation, calculate the base/acid ratio at pH 7. In 30 words or less, what is the significance of the predominant form at pH 7 in relation to the formation of the DNA double helix?arrow_forward
- Report the isoelectric point of the peptide, Gly-Asp-Lys-Ile?arrow_forwardOrnithine is an amino acid that is not used in the synthesis of proteins, but is an important intermediate in several metabloic pathways including the urea cycle and the synthesis of polyamines. It has a perfectly ordinary terminal amino group and terminal carboxyl group like any other amino acid (so use the pKas for those groups given on your amino acids handout), and a side chain with a single ionizable side group with a pKa of 10.3. If ornithine is placed in solution at pH 7.0, it has a net charge of +1. What would the net charge on this amino acid be if the pH of the solution was raised to pH 12.0? Please explain your reasoning.arrow_forwardWhich one is Second prominent form of arginine at pH 6.0 in the picture below?arrow_forward
- An amino acid's guadinine side chain has a pKa of 12.5 what is the ratio of uncharged to charged guanidino at pH10.5arrow_forwardChemistry Estimate the pI of a dipeptide Cys-Asp assuming that the pKa values for αα-NH3+, αα-COOH, side chain of Cys and side chain of Asp are 8.0, 3.5, 8.5, and 3.9, respectively. Round your answer to one decimal place.arrow_forwardAt very low pH, alanine is a diprotic acid that can be represented as H3N1-CH(CH3)-COOH. The pKa of the carboxyl group is 2.3, and the pKa of the UNH1 3 group is 9.7.(a) At pH 7, what fraction of the amino acid molecules dissolved in an          aqueous solution will have the form            H3N1-CH(CH3)-COO2?(b) What fraction of the molecules at this pH will havethe form                          H2N-CH(CH3)-COOH?arrow_forward
- Draw the peptide CHEMISTRY. a. What is the full name and 3-letter abbreviation of this peptide? b. Give the different forms (charges) of the peptide as it is titrated from pH 1.5 until pH 12.0. c. What is the isoelectric point of the peptide?arrow_forwardThe pKa for the side chain amino group in lysine is 10.4. If we were working at physiological pH 7.4, what would be the ratio of the protonated to unprotonated versions of lysine?  a. 1000:1  b. 3:1  c. 1:1000  d. 1:3arrow_forwardCalculate the avergae charge on arginine when pH = 9.2 (hint: find the average charge for each inoizable group and sum these together.arrow_forward
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