Essential Organic Chemistry (3rd Edition)
3rd Edition
ISBN: 9780321937711
Author: Paula Yurkanis Bruice
Publisher: PEARSON
expand_more
expand_more
format_list_bulleted
Concept explainers
Videos
Textbook Question
Chapter 17.1, Problem 1P
- a. Explain why, when the imidazole ring of histidine is protonated, the double-bonded nitrogen is the nitrogen that accepts the proton. (Hint: Localized electrons are more apt to be protonated than delocalized electrons.)
- b. Explain why, when the guanidino group of arginine is protonated, the double-bonded nitrogen is the nitrogen that accepts the proton.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solution
Students have asked these similar questions
How Ranitidine will be syntesized? give full reaction
In the case of serine, threonine and tyrosine they have the -OH group in their residue. I'm wondering even though all of them has the -OH groups in their residue. but only the tyrosine has the pKa value with the -OH grouup.
Supposing reagents for other Rh antigens are present and considering the nature of Rh Blood group antibodies, what additional step can be done to properly demonstrate the expected reaction using the forward slide method?
Chapter 17 Solutions
Essential Organic Chemistry (3rd Edition)
Ch. 17.1 - a. Explain why, when the imidazole ring of...Ch. 17.2 - Prob. 2PCh. 17.3 - Prob. 3PCh. 17.3 - Prob. 4PCh. 17.3 - Prob. 6PCh. 17.4 - Calculate the pI of each of the following amino...Ch. 17.4 - a. Which amino acid has the lowest pI value? b....Ch. 17.5 - What aldehyde is formed when valine is treated...Ch. 17.5 - Prob. 10PCh. 17.5 - Prob. 11P
Ch. 17.5 - Prob. 12PCh. 17.6 - Prob. 13PCh. 17.6 - What amino acid would be formed using the...Ch. 17.6 - What amino acid would be formed when the aldehyde...Ch. 17.7 - Pig liver esterase is an enzyme that catalyzes the...Ch. 17.8 - Prob. 17PCh. 17.8 - Prob. 18PCh. 17.8 - Prob. 19PCh. 17.8 - Prob. 20PCh. 17.10 - Prob. 21PCh. 17.10 - Prob. 22PCh. 17.10 - Why does cyanogen bromide not cleave on the C-side...Ch. 17.10 - Prob. 24PCh. 17.10 - Prob. 26PCh. 17.12 - Prob. 27PCh. 17.13 - a. Which would have the greatest percentage of...Ch. 17 - Draw the predominant form of the following amino...Ch. 17 - What is the pI of serine?Ch. 17 - Prob. 31PCh. 17 - Prob. 32PCh. 17 - Which would have a higher percentage of negative...Ch. 17 - Draw the form of aspartate that predominates at...Ch. 17 - Prob. 35PCh. 17 - A professor was preparing a manuscript for...Ch. 17 - a. Why is the pKa of the glutamate side chain...Ch. 17 - Prob. 38PCh. 17 - Determine the amino acid sequence of a polypeptide...Ch. 17 - Prob. 40PCh. 17 - Prob. 41PCh. 17 - Three peptides were obtained from a trypsin...Ch. 17 - Prob. 43PCh. 17 - After the polypeptide shown here was treated with...Ch. 17 - The disulfide bridges of a polypeptide were...Ch. 17 - -Amino acids can be prepared by treating an...Ch. 17 - Reaction of a polypeptide with carboxypeptidase A...Ch. 17 - Prob. 48PCh. 17 - Prob. 49PCh. 17 - Show how valine can be prepared by a. a Strecker...Ch. 17 - Prob. 51PCh. 17 - Why is proline never found in an -helix?Ch. 17 - Determine the amino acid sequence of a polypeptide...Ch. 17 - Prob. 55PCh. 17 - A chemist wanted to test his hypothesis that the...Ch. 17 - A normal polypeptide and a mutant of the...
Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, chemistry and related others by exploring similar questions and additional content below.Similar questions
- Leuprolide is a synthetic nonapeptide used to treat both endometriosis in women and prostate cancer in men. (a) Both C-terminal and N-terminal amino acids in leuprolide have been structurally modified. Identify the modifications. (b) One of the nine amino acids in leuprolide has d stereochemistry rather than the usual L. Which one? (c) Write the structure of leuprolide using both one- and three-letter abbreviations. (d) What charge would you expect leuprolide to have at neutral pH?arrow_forwardWhat would be the structure of the two anomers of idopyranose in HAWORTH FORMULA? a. its beta-anomer and b. its alpha-anomerarrow_forwardIn a paragraph form provide the experimental procedure of the reaction of oxazetidine-containing peptides and α-ketoacid that will result in protein that contain native serine residuesarrow_forward
- According to the paper, F486 is a phenylalanine residue (i.e., an amino acid that is part of a chain that forms a protein) on SARS-CoV-2. It has an important interaction with ACE2 (best seen in Fig. 1(C) and Fig. 2(A)). Looking at this phenylalanine and the green residues surrounding it, which statement best describes the interaction that could be occurring? a) It forms a hydrogen bond with Y83. b) It forms a dipole-dipole interaction with M82. c) It forms London dispersion forces with surrounding residues. d) It encounters repulsions from surrounding residues.arrow_forwardThymine is one of the heterocyclic bases found in DNA. Do you expect thymine to bearomatic? Explainarrow_forwardBased on the given figure,a. what is the possible identity of the amino acid?b. what is the isoelectric point of AAc. what is the pKa corresponding to the dissociation of alpha carboxylic groupd. where is the region or point where AA is predominantly present as a (-2) charged speciese. where is the effective buffering range for the amino acid on the acidic regionarrow_forward
- would chymotrypsin to be most active at a pH of 4.5, 7.8, or 10.0?arrow_forwardGlycine has pKa values of 2.34 and 9.60. At what pH does glycine exist in the indicated form?arrow_forward1a. suggest a test you will use to show that a given food substance contains protein. b. show how you will use i. modified Gabriels synthesis ii. Streckers synthesis to prepare phenylalanine in the laboratory. 2a. Describe in details how you will determine the primary structure of protein. b. You have been given a mixture of lysine, histidine and cysteine. The isoelectric point of the amino acids are as follows, Histidine 7.64 Lysine 9.74 Cysteine 5.02 Show how you will separate the mixture into the pure forms. State and describe any instrument that you will use to separate the components. 3a. A decapeptide has the following amino acid composition, Ala2, Arg, Cys, Glu, Gly, Leu, Lys, Phe, Val Partial hydrolysis yields the following tripeptides, Cys-Glu-Leu +Gly-Arg-Ala +Lys-Val-Phe-Gly Reaction of the decapeptide with 2,4-dinitrofluorobenzene yields 2,4-dinitrophenylsine. From the experimental data, deduce the primary structure of the…arrow_forward
- How do you account for the fact that the -COOH group of the conjugate acid of alanine is a stronger acid than the -COOH group of propanoic acid?arrow_forwardExplain why, when the imidazole ring of histidine is protonated, the double-bonded nitrogen is the nitrogen that accepts the proton.arrow_forwardAssuming the oligopeptide ALPHAHELICKS forms one continuous alpha-helix, the carbonyl oxygen of the glutamic acid residue is hydrogen-bonded to the hydrogen in the amide nitrogen of??arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
Organic Chemistry: A Guided InquiryChemistryISBN:9780618974122Author:Andrei StraumanisPublisher:Cengage Learning
EBK A SMALL SCALE APPROACH TO ORGANIC LChemistryISBN:9781305446021Author:LampmanPublisher:CENGAGE LEARNING - CONSIGNMENT
Organic Chemistry: A Guided Inquiry
Chemistry
ISBN:9780618974122
Author:Andrei Straumanis
Publisher:Cengage Learning
EBK A SMALL SCALE APPROACH TO ORGANIC L
Chemistry
ISBN:9781305446021
Author:Lampman
Publisher:CENGAGE LEARNING - CONSIGNMENT
Biomolecules - Protein - Amino acids; Author: Tutorials Point (India) Ltd.;https://www.youtube.com/watch?v=ySNVPDHJ0ek;License: Standard YouTube License, CC-BY