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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 22.4, Problem 13P
Interpretation Introduction
Interpretation:
The
Concept introduction:
The isoelectric point (
The value of
If the amino acid has ionizable side chain, then the
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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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- A protein has a number of aspartyl and gluatmyl residues, what would be the expected pI for this protein?   a. Basic pI   b. Neutral pI   c. Cannot be determined    d. Acidic pIarrow_forwardWould serine or cysteine be the better antidote against heavy metals? Briefly rationalize your answer.arrow_forwardDraw Tryptophan in a peptide bond. Explain all of the bonds using valence bond theory (VBT). Next, explain where VBT fails and how molecular orbital theory is a better description of key regions of this amino acid and the peptide bonds it forms with other residuesarrow_forward
- The configuration of the chiral center in a-amino acids is most commonly specified using the d,l convention. It can also be identified using the R,S convention . Does the chiral center in l-serine have the R or S configuration?arrow_forwardWhere would you expect to find a cysteine unit in the tertiary structure of a water-soluble globular protein? Why?  Group of answer choices on the interior, because cysteine's side-chain is polar on the exterior, because cysteine's side-chain is polar on the exterior, because cysteine's side-chain is hydrophobic on the interior, because cysteine's side-chain is hydrophobicarrow_forwardCan you explain how to determine their IMFsarrow_forward
- A 1.00-mg sample of a pure protein yielded on hydrolysis 0.0165 mg of leucine and 0.0248 mg of isoleucine. What is the minimum possible molar mass of the protein? (MMleucine=MMisoleucine=131g/mol)arrow_forwardUsing both three- and one-letter codes for amino acids, write the structures of all possible peptides containing the following amino acids: (a) Val, Ser, Leu (b) Ser, Leu2, Proarrow_forwardAs stated, proteins are stereochemically pure because only a single enantiomer of each amino acid building block is used by nature. How many stereoisomers are possible for a chain of only 3 chiral amino acids if both enantiomers of the amino acids are used? 1. 2 2. 4 3. 8 4. 16arrow_forward
- How many of the -amino acids shown in Table 26-1 contain aromatic rings? How many contain sulfur? How many contain alcohols? How many contain hydrocarbon side chains?arrow_forwardChemistry 1a. The lack of an asymmetric carbons and ease of rotation make glycine rich protein sequences: a. Fibrous b. Helical c. Cyclic d. Flexible e. Globular 1b. Introducing D-amino acids into peptides can be useful as a strategy to: a. Change pKa b. Reduce thermal stability c. Alter ionic strength d. Slow degradation e. Increase solubility 1c. Cellulose is not useful dietary carbohydrate because humans: a. Don’t have sufficient non-mitochondrial ATP b. Lack a 1,4-beta glycosidase c. Can’t digest branched chain carbohydrates d. Loose lactase as they mature e. Can’t absorb pentise subunitsarrow_forward3. Draw the tripeptide Alanine-Cysteine-Serine (R1 = CH3, R2 = CH2SH, R3 = CH2OH) under the following pH conditions and list the net charge on the protein. A. pH= 1 Net charge? B. pH=7 Net charge? C. pH=12 Net charge?arrow_forward
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