Organic Chemistry (9th Edition)
9th Edition
ISBN: 9780321971371
Author: Leroy G. Wade, Jan W. Simek
Publisher: PEARSON
expand_more
expand_more
format_list_bulleted
Concept explainers
Question
Chapter 23.16C, Problem 23.45P
Interpretation Introduction
Interpretation: The diagram which shows hydrogen-bonded guanine-cytosine and adenine-thymine pairs are to be drawn and the reason as to why the hydrogen bonds involved in the pairing are particularly strong is to be stated.
Concept introduction: A hydrogen bond is a strong type of bond or electrostatic attraction which mainly occurs when hydrogen atom is bound to a more electronegative atom. It is of two types; intramolecular hydrogen bonding and intermolecular hydrogen bonding.
To determine: The diagram which shows hydrogen-bonded guanine-cytosine and adenine-thymine pairs and the reason as to why the hydrogen bonds involved in the pairing are particularly strong.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solution
Students have asked these similar questions
Refer to the bar graph below, Explain why the n→π* interactions contributes more to the overall stabilization of the protein than all the other interactions(C-H-O hydrogen bond,π-π interactions, C5 Hydrogen Bonds, Cation-π interactions, Sulfur-arene interactions, Anion-π interactions, Chalcogen bonds, X-H-π interactions) even though n→π* is the weaker interaction.
Explain why that's the case for EACH of the bonds.
I.e
Why n→π* interactions contribute more to the overall stabilization of the protein than C-H-O hydrogen bonds, even though n→π* is the weaker interaction.
Why n→π* interactions contribute more to the overall stabilization of the protein than π-π interactions even though n→π* is the weaker interaction.
Why n→π* interactions contribute more to the overall stabilization of the protein than C5 Hydrogen Bonds, even though n→π* is the weaker interaction.
Why n→π* interactions contribute more to the overall stabilization of the protein than Cation-π interactions, even though…
23. The amino acid side chains of 17 of the 20 most common amino acids are shown below. Which are aromatic side chains? Type their corresponding letter in alphabetical order.
A1c
Select ONE peptide linkage and draw a circle around all of the atoms that
would lie in a single plane.
H R2
|
H
H;Ñ.
||
C.
N
R, H
H
R3 H
Ilt.
O=0
Chapter 23 Solutions
Organic Chemistry (9th Edition)
Ch. 23.2 - Prob. 23.1PCh. 23.3A - Prob. 23.2PCh. 23.3A - Prob. 23.3PCh. 23.3B - Draw and name the enantiomers of the sugars shown...Ch. 23.3B - Prob. 23.5PCh. 23.3C - Prob. 23.6PCh. 23.4 - Draw the Haworth projection for the cyclic...Ch. 23.4 - Prob. 23.8PCh. 23.4 - Prob. 23.9PCh. 23.4 - Prob. 23.10P
Ch. 23.4 - Prob. 23.11PCh. 23.5 - Prob. 23.12PCh. 23.5 - Prob. 23.13PCh. 23.6 - Prob. 23.14PCh. 23.6 - Prob. 23.15PCh. 23.7 - Prob. 23.16PCh. 23.7 - Prob. 23.17PCh. 23.7 - Two sugars, A and B, are known to be glucose and...Ch. 23.7 - Prob. 23.19PCh. 23.8 - Prob. 23.20PCh. 23.8 - Prob. 23.21PCh. 23.8 - Prob. 23.22PCh. 23.8 - Prob. 23.23PCh. 23.8 - Prob. 23.24PCh. 23.9 - a. Show the product that results when fructose is...Ch. 23.9 - Prob. 23.26PCh. 23.9 - Prob. 23.27PCh. 23.9 - Prob. 23.28PCh. 23.10 - Prob. 23.29PCh. 23.10 - Prob. 23.30PCh. 23.10 - Prob. 23.31PCh. 23.11 - Prob. 23.32PCh. 23.11 - The Wohl degradation, an alternative to the Ruff...Ch. 23.11 - Prob. 23.34PCh. 23.11 - Prob. 23.35PCh. 23.12A - Prob. 23.36PCh. 23.12A - Give an equation to show the reduction of Tollens...Ch. 23.12A - Prob. 23.38PCh. 23.12B - Prob. 23.39PCh. 23.12C - Prob. 23.40PCh. 23.12C - Prob. 23.41PCh. 23.13A - Prob. 23.42PCh. 23.15 - Cytosine, uracil, and guanine have tautomeric...Ch. 23.15 - a. An aliphatic aminoglycoside is relatively...Ch. 23.16C - Prob. 23.45PCh. 23 - Prob. 23.46SPCh. 23 - Prob. 23.47SPCh. 23 - Prob. 23.48SPCh. 23 - Prob. 23.49SPCh. 23 - Prob. 23.50SPCh. 23 - Prob. 23.51SPCh. 23 - Prob. 23.52SPCh. 23 - Prob. 23.53SPCh. 23 - Prob. 23.54SPCh. 23 - Prob. 23.55SPCh. 23 - Prob. 23.56SPCh. 23 - Prob. 23.57SPCh. 23 - Prob. 23.58SPCh. 23 - Prob. 23.59SPCh. 23 - Prob. 23.60SPCh. 23 - Prob. 23.61SPCh. 23 - Prob. 23.62SPCh. 23 - Prob. 23.63SPCh. 23 - Draw the structure of a four-residue segment of...Ch. 23 - Retroviruses like HIV, the pathogen responsible...Ch. 23 - Prob. 23.66SPCh. 23 - Prob. 23.67SP
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
- Refer to the bar graph below, Explain why the n→π* interactions contributes more to the overall stabilization of the protein than all the other interactions(C-H-O hydrogen bond,π-π interactions, C5 Hydrogen Bonds, Cation-π interactions, Sulfur-arene interactions, Anion-π interactions, Chalcogen bonds, X-H-π interactions) even though n→π* is the weaker interaction. Explain why that's the case for EACH of the bonds. Why n→π* interactions contribute more to the overall stabilization of the protein than Sulfur-arene interactions, even though n→π* is the weaker interaction. Why n→π* interactions contribute more to the overall stabilization of the protein than Anion-π interactions, even though n→π* is the weaker interaction. Why n→π* interactions contribute more to the overall stabilization of the protein than Chalcogen bonds, even though n→π* is the weaker interaction. Why n→π* interactions contribute more to the overall stabilization of the protein than X-H-π interactions, even…arrow_forwardTo be a nucleotide OR protein it MUST have a nitrogenous group. This answer is wrong.arrow_forwardRefer to the bar graph below, Explain why e.g. the n→π* interactions contribute more to the overall stabilization of the protein than all the other interactions(C-H-O hydrogen bond,π-π interactions, C5 Hydrogen Bonds, Cation-π interactions, Sulfur-arene interactions, Anion-π interactions, Chalcogen bonds, X-H-π interactions) even though n→π* is the weaker interaction. Explain why they contribute more than EACH bond.arrow_forward
- Identify the following antioxidant molecule. A. alpha tocopherol hydroquinone B.dehydroascorbic acid CH3 CH3 C. alpha tocopherol semi-quinone \ / D. ascorbic acid C = C E. alpha tocopherol quinone / \ : O – C C – O CH3 \\ // \ / C – C C – CH2–CH2–CH2–CH–CH2–CH2–CH2–CH–CH2–CH2–CH2–CH–CH3 / \ / l l l CH3 CH2– CH2…arrow_forwardQ1. Would an amino acid with the given side chain be most likely to be found in the hydrophobic or hydrophilic region of a protein? Circle one below. A. B. C. -CH₂-CH-CH3 I CH3 O -CH2-C-NH2 -CH-CH3 | ОН Circle one: Hydrophilic region // Hydrophobic region Circle one: Hydrophilic region // Hydrophobic region Circle one: Hydrophilic region // Hydrophobic regionarrow_forwardIdentify the features of the two bonded amino acids depicted in the image. HOHH | || | | N-C-C-N-C-C CH CH₂2 CH₂2 CH₂ CH₂ I I CH₂ CH₂ NH₂+ O OH Answer Bank hydrophilic side chain hydrophobic side chain peptide bond carboxyl group amino grouparrow_forward
- Now consider alanine as a whole molecule. Use the Ką values from the chart above, and your understanding of the relationships among Ka, pH, and charge to select the predominant form of alanine that would exist at the pH indicated below. Note some choices may not be used and some may be used more than once. A. NH3+ D. NH3+ pH = 1 pH = 5 pH = 7 pH = 11 CH3 H CH3 1 H COOH COO- B. NH₂ E. NH₂ A D D с CH3 + C H - CH₂™ C | H COOH COO- C. NH₂ F. NH₂ CH3 + -C H - CH₂™ C I H COO- COOHarrow_forwardLysine and tryptophan are two amino acids that contain an additional N atom in the R group bonded to the a carbon. While lysine is classified as a basic amino acid because it contains an additional basic N atom, tryptophan is classified as a neutral amino acid. Explain why this difference in classification occurs.arrow_forwardAlthough the bond energy for the hydrogen bond in a vacuum is estimated to be about 20 kJ/mol, we find that each hydrogen bond in a folded protein contributes much less--probably less that 5 kJ/mol--to the enthalpy of protein stabilization. Suggest an explanation for this difference. Explain briefly.arrow_forward
- ogical Marcomalee Identifying specific interactions between residues in a protein Imagine the main chain of a protein bends back on itself, so that two amino acid residues R, and R, come close to each other. Here's what R, looks like: -CH- -- CH2 OH O yes Could R, form a hydrogen bond with R₂ at physiological pH, if R₂ were the right kind of residue? O no If you said R, could form a hydrogen bond with R2, what would R₂ have to be? If there's only one possibility, write its 3-letter code. If there is more than one possibility, write the 3-letter code of any of them. 0 Explanation Check ㅎ C S A * 2 # 3 $ 4 Z W M S X Ő % Λ 25 & 6 7 E R T Y U D C dill LLC. All Rights Reserved. Terms of Use Privacy Center NP 8 A 9 O 0 LL F G H J K L V B N M P altarrow_forwardQ1. Eticlopride is a dopamine antagonist, which can block dopamine receptor sites and influence levels of dopamine. The molecule is involved in a number of intermolecular interactions with amino acids in the G protein-coupled receptor. о но ČI Eticlopride i) Draw a suitable diagram to indicate where the following amino acids might interact with the molecule: phenylalanine; valine; histidine; tyrosine. In your answer, please draw the amino acids and show the interaction. ii) For each interaction you have shown, state the nature of that interaction (e.g. H- bonding, pi-pi etc.)arrow_forwardWhich of these amino acids has a hydrophobic side chain?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
Organic ChemistryChemistryISBN:9781305580350Author:William H. Brown, Brent L. Iverson, Eric Anslyn, Christopher S. FootePublisher:Cengage Learning
Introduction to General, Organic and BiochemistryChemistryISBN:9781285869759Author:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar TorresPublisher:Cengage Learning
Chemistry: Matter and ChangeChemistryISBN:9780078746376Author:Dinah Zike, Laurel Dingrando, Nicholas Hainen, Cheryl WistromPublisher:Glencoe/McGraw-Hill School Pub Co
Chemistry for Today: General, Organic, and Bioche...ChemistryISBN:9781305960060Author:Spencer L. Seager, Michael R. Slabaugh, Maren S. HansenPublisher:Cengage Learning
Organic Chemistry: A Guided Inquiry
Chemistry
ISBN:9780618974122
Author:Andrei Straumanis
Publisher:Cengage Learning
Organic Chemistry
Chemistry
ISBN:9781305580350
Author:William H. Brown, Brent L. Iverson, Eric Anslyn, Christopher S. Foote
Publisher:Cengage Learning
Introduction to General, Organic and Biochemistry
Chemistry
ISBN:9781285869759
Author:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres
Publisher:Cengage Learning
Chemistry: Matter and Change
Chemistry
ISBN:9780078746376
Author:Dinah Zike, Laurel Dingrando, Nicholas Hainen, Cheryl Wistrom
Publisher:Glencoe/McGraw-Hill School Pub Co
Chemistry for Today: General, Organic, and Bioche...
Chemistry
ISBN:9781305960060
Author:Spencer L. Seager, Michael R. Slabaugh, Maren S. Hansen
Publisher:Cengage Learning