Study Guide for Campbell Biology
11th Edition
ISBN: 9780134443775
Author: Lisa A. Urry, Michael L. Cain, Steven A. Wasserman, Peter V. Minorsky, Jane B. Reece, Martha R. Taylor, Michael A. Pollock
Publisher: PEARSON
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Textbook Question
Chapter 4, Problem 11TYK
Cis-trans isomers require
- a. highly polar
functional groups . - b. carbon-carbon double bonds.
- c. branched carbon chains.
- d. ring-shaped carbon skeletons.
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Describe why G-C bonding is stronger than A-T. Why is it important?
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Which of the following statement about proteins is correct
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Chapter 4 Solutions
Study Guide for Campbell Biology
Ch. 4 - How did Millers classic experiment relate to the...Ch. 4 - Define structural isomers, cis-trans isomers, and...Ch. 4 - Practice recognizing the functional groups by...Ch. 4 - Construct a concept map that illustrates your...Ch. 4 - Fill in the following table to review the...Ch. 4 - Carbons valence of four most directly results from...Ch. 4 - Prob. 2TYKCh. 4 - Hydrocarbons are not soluble in water because a....Ch. 4 - Prob. 4TYKCh. 4 - Which of the following is not true of an...
Ch. 4 - Enantiomers are a. molecules that are mirror...Ch. 4 - Which statement is not true about structural...Ch. 4 - Prob. 8TYKCh. 4 - The orbitals of a carbon atom form a(n) a....Ch. 4 - The following ribose molecule contains how many...Ch. 4 - Cis-trans isomers require a. highly polar...Ch. 4 - The chemical group that can cause an organic...Ch. 4 - The chemical group that confers acidic properties...Ch. 4 - Structural isomersCh. 4 - Prob. 2TYKMCh. 4 - can have enantiomersCh. 4 - carboxylic acidCh. 4 - can make cross-link in proteinCh. 4 - hydrophilicCh. 4 - hydrocarbonCh. 4 - amino acidCh. 4 - organic phosphateCh. 4 - aldehydeCh. 4 - amineCh. 4 - ketone
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- A polypeptide with a net positive charge at physiologic pH (~7.4) most likely contains amino acids with R groups of what type? a. Acidic R groups b. Aromatic R groups c. Aliphatic R groups d. Basic R groupsarrow_forwardOn the image below, label the structures below (image is in color-view it online). "Not present" is an acceptable answer. a. Alpha helix b. Beta sheet C. Hydrophobic core d. Random coil е. Reasonable location for a proline f. Draw in the appropriate hydrogen bonds for stabilizing the secondary structure for one alpha helix and one beta sheet. If the structure is not present, write that here.arrow_forwardDraw a diagram of a peptide bond in the cis and trans configurations. Show the contributing resonance structures and the composite resonance structure for each configuration.arrow_forward
- Which of the following correctly describes peptide bonds? * A. They are a special type of amide bond. B. They are very stable bonds. C. They form when water separates from an amino group and a carboxylic acid. D. They are a bond that shows resonance. E. All of these Which group consists only of amino acids with polar side chains? * A. serine, threonine, and leucine B. serine, threonine, and cysteine C. serine, threonine, and valine D. serine, threonine, and isoleucinearrow_forwardWhat type of interactions is primarily responsible for the creation of the following type of a) Covalent Bonding b) Ionic Interactions c)H-bonding d) Hydrophobic interactions structures? 1. a in the formation of a protein's primary structure 2. C in the formation of an alpha helix 3. d in the formation of a protein's tertiary structure 4. Which of the following polypeptides is capable of forming the most stable alpha helix? a) EEEEEE at pH 7 d) KKKKKK at pH 2 e) PPPPPP at pH 7 b) KKKKKKK at pH 7 (c) EEEEEE at pH 2 5/6. Explain your answer to the previous question. 7. Which of the following is NOT true of a collagen helix or collagen? a) A collagen helix cannot contain prolines. b) A collagen helix has a special amino acid called Hyp c) Collagen is a fibrous protein d) In collagen three helices come together to form a triple helix 8. Which of the following CANNOT make a H-bond. More than one can be circled. a) N-HO-C b) N…H-O-H Ⓒ)C=O....N-C d)C=O....H-O- 9. Which of the following…arrow_forwardDefine the following terms: a. salt bridge b. allosteric transition c. molecular disease d. protein denaturation e. α-helixarrow_forward
- Draw and label the dinucleotide AT as follows: A. 5’ and 3’ ends B. Phosphodiester bond C. N-glycosidic bondsarrow_forward1) Describe the importance of the amino acids in the structure such as the alpha helix in the secondary structure; the beta-sheet and the alpha helix in the final tertiary structure. 2) A photo of a 3D tertiary structure model of your protein using paper.arrow_forwardWhich of the following is incorrect? (₁) a. A heterodimer is composed by two identical polypeptide chains b. The polypeptide chains in a multimeric protein are called subunits A homotrimer can be represented with the Greek letter alpha with a sub-index 3 d. Monomeric proteins do not have quaternary structure c.arrow_forward
- 1.a.If this molecule was the side chain of an amino acid, in a protein, what tertiary structure stabilizers could be present? b.Make a key and use color to highlight what part of you structure can be stabilized in each manner?arrow_forwarda. What is a heterocyclic amine? What was the most interesting example you found out about? Why was it interesting? b. DNA and RNA are heterocyclic amines with Nitrogen in the center. If sulfur were in the middle of the ring instead of Nitrogen how would this affect the ability to H-bond? c. Show the structure of 2 neurotransmitters. What are some of the interactions you found out about it.arrow_forwardIn most cases the peptide bond is in the trans conformation. What statement below best explains this observation? a) The peptide bond has double bond character that prevents free rotation. b) In the cis conformation the R groups cause steric hindrance. c) In the trans conformation the carbonyl oxygen and the amine hydrogen can participate in hydrogen bonding. d) In the trans conformation the angle strain is reduced. e) All of the above explain the observation. while all statements might be true they do not explain the phenomenonarrow_forward
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