Biology
12th Edition
ISBN: 9781260494570
Author: Raven, Peter
Publisher: MCGRAW-HILL HIGHER EDUCATION
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Textbook Question
Chapter 3, Problem 2S
Hydrogen bonds and hydrophobic interactions each play an important role in stabilizing and organizing biological macromolecules. Consider the four macromolecules discussed in this chapter. Describe how these affect the form and function of each type of macromolecule. Would a disruption in the hydrogen bonds affect form and function? Hydrophobic interactions?
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For each of the following pairs of amino acids, identify the strongest type of intermolecular forces involved when the side chains interact. Explain in terms of the chemical structures of the amino acid side chains. Use the following list: disulfide bridge, hydrogen bonding, hydrophobic interaction, or salt bridge.
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Chapter 3 Solutions
Biology
Ch. 3.1 - Describe the relationship between functional...Ch. 3.1 - Recognize the different kinds of isomers.Ch. 3.1 - Prob. 3LOCh. 3.2 - Prob. 1LOCh. 3.2 - Prob. 2LOCh. 3.3 - Prob. 1LOCh. 3.3 - Prob. 2LOCh. 3.3 - Prob. 3LOCh. 3.3 - Prob. 4LOCh. 3.4 - Prob. 1LO
Ch. 3.4 - Prob. 2LOCh. 3.4 - Prob. 3LOCh. 3.5 - Prob. 1LOCh. 3.5 - Prob. 2LOCh. 3.5 - Prob. 3LOCh. 3 - Prob. 1UCh. 3 - Why are carbohydrates important molecules for...Ch. 3 - Plant cells store energy in the form of ______,...Ch. 3 - Prob. 4UCh. 3 - A molecule of DNA or RNA is a polymer of a....Ch. 3 - Prob. 6UCh. 3 - What monomers make up a protein? a....Ch. 3 - A triglyceride is a form of _______ composed of...Ch. 3 - You can use starch or glycogen as an energy...Ch. 3 - Which of the following is NOT a difference between...Ch. 3 - Prob. 3ACh. 3 - A mutation that alters a single amino acid within...Ch. 3 - Two different proteins have the same domain in...Ch. 3 - What aspect of triglyceride structure accounts for...Ch. 3 - The spontaneous formation of a lipid bilayer in an...Ch. 3 - Prob. 1SCh. 3 - Hydrogen bonds and hydrophobic interactions each...Ch. 3 - Prob. 3S
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- Which of the following types of molecular interactions play a role in protein folding? Select all that apply. A.)Hydrophobic interactions B.)Van der Waals attraction C.)Hydrogen bonds D.)Covalent bondsarrow_forwardGive the 4 types of Biomolecules - their chemical composition, monomer, function/s, types and 2 examples for each type (1 example is for plants and the other example is for animals).arrow_forwardWhich of the following (could be more than one) would not be a rational explanation for why the three-dimensional structure of a protein is driven and stabilized largely by noncovalent rather than covalent bonds?a) Proteins may be degraded for energy, and if their three-dimensional structures were heldtogether by mostly covalent bonding, this might be too difficult to accomplishb) Proteins will need to be unfolded to cross biological membrane, and if their three-dimensionalstructures were held together by mostly covalent bonding, this might be too difficult toaccomplish.c) Protein function (transport, enzyme catalysis, etc...) may require flexibility in the three-dimensional structure to allow for conformational change, and if protein three-dimensionalstructure were held together by mostly covalent bonding, this might be too difficult toaccomplish.d) All of the answer choices are rational explanations for why the three-dimensional structure of protein is driven and stabilized largely…arrow_forward
- The properties and biological activities of biomolecules are largely determined by their functional groups. In each of the following compounds below, circle and identify by name each functional group.arrow_forwarda. what general category would you place this molecule in of the four categories of biomolecules? b. List 5 functional groups you see in this molecule?arrow_forwardThe most important contribution to the stability of a globular protein's conformation appears to be the: a.) entropy increase from the decrease in ordered water molecules forming a solvent shell around it. b.) maximum entropy increase from ionic interactions between the ionized amino acids in a protein. c.) sum of free engeries of formation of may weak interactions between its polar amino acids and surrounding water.arrow_forward
- In a subunit of a protein, arginine and aspartic acid have an ionic interaction between their side chains. Part a) If arginine is changed to glutamic acid, would the ionic interaction's stability increase, decrease, or not change and what effect would it have on the protein structure? Explain why. Part b) If arginine is changed to lysine, would the ionic interaction's stability increase, decrease, or not change and what effect would it have on the protein structure? Explain why. Part c) If arginine is changed to isoleucine, would the ionic interaction's stability increase, decrease, or not change and what effect would it have on the protein structure? Explain why.arrow_forwardWhat are the similarities and differences of intermolecular interactions that stabilize secondary versus tertiary structure? Think about types of interactions, side-chain versus backbone interactions, and proximity of the residues involved.arrow_forwardWhy is the 3-Dimensional structure important for protein function? What factors or agents can denature protein structure? Give examples (more than one factor) Why denaturation affect the function of proteins? Explain the structure - function relationship.arrow_forward
- What are the forces that determine the folding of a macromolecule into a unique shape?arrow_forwardDescribe, identify, and DRAW the monomers (e.g. what is typically illustrated as a hexagon?) andpolymers of:a. Proteinsb. Carbohydratesc. Lipids Identify the type of chemical bonds that join the monomers of:a. Proteins (describe the structure and function of a polymer)b. Carbohydrates (describe the structure and function of a polymer)c. Lipids Identify the portions of the cell membrane (phospholipid bi-layer) that area. Hydrophobicb. Hydrophilicc. Polard. Non-polararrow_forwardName and describe the four weak chemical interaction that occurs in biomolecules.arrow_forward
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