BIOLOGY
12th Edition
ISBN: 9781260169614
Author: Raven
Publisher: RENT MCG
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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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Hydrogen bonds and hydrophobic interactions play important roles in
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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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Hydrogen bonds and hydrochloric interactions play important roles in stabilizing and organizing biological macromolecules. Describe how Hydrogen bonds and hydrochloric interactions affects the form and function of proteins.
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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- Disulfide bonds help to stabilize the three-dimensional structure of proteins. What amino acids are involved in the formation of disulfide bonds? Does the formation of a disulfide bond increase or decrease entropy (ΔS)?arrow_forwardLabel: 1) the type of chemical bonds between the amino acids (e.g. covalent bond, ionic bond, metallic bond) 2) the type of interparticle forces of attraction occurring within the protein and with its environment *Indicate at least four observed interparticle forces of attraction *pink - negatively charged, blue - positively charged, yellow - nonpolar and uncharged, green - polar and uncharged *[See example picture] The chemical bond (shown by the arrow) is depicted as a line between the amino acids. Interparticle forces of attraction, such as the one between Phe and Glu (boxed), are not represented by lines but rather by the proximity of amino acids.arrow_forwardDiscuss the different structures (primary, secondary, tertiary, and Quaternary structures) of protein. What are the five factors that promote protein folding and stability. (Hint: One factor is the Hydrogen bond). Extra Hint: Another factor is the Hydrophobic effect.arrow_forward
- Give 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_forwardWhen a small, globular protein unfolds, which of the following are true? (SELECT ALL THAT APPLY) Choice 1 of 6: the temperature must increase Choice 2 of 6: the entropy of the peptide backbone increases Choice 3 of 6: the entropy of the solvent waters increases Choice 4 of 6: H bonds between peptide backbone atoms must break Choice 5 of 6: new attractive interactions form between water and side chains Choice 6 of 6: a detergent molecule must be addedarrow_forward
- The 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_forwardIn 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_forward
- Why 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_forwardIn studying a particular biomolecule (protein, nucleic acid, carbohydrate, lipid), a biochemist needs to separate/ purify it from other biomolecules in the sample. However, looking at the monomeric subunits of a biomolecule, one should have an idea about the characteristics of the molecule that would allow to separate/purify it from other molecules. On what basis can you separate: a. amino acids from fatty acids? b. nucleotides from glucose?arrow_forwardWhich of the following statements best describes the hydrophobic character of bacteriorhodopsin (2BRD)? Both the interior and exterior of the protein are hydrophobic, including the central core of the trimer. Both the interior and exterior of the protein are hydrophilic, including the central core of the trimer. Both the interior and exterior of the protein are hydrophilic, but the central core of the trimer is hydrophobic. Both the interior and exterior of the protein are hydrophobic, but the central core of the trimer is hydrophilic.arrow_forward
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Biomolecules - Protein - Amino acids; Author: Tutorials Point (India) Ltd.;https://www.youtube.com/watch?v=ySNVPDHJ0ek;License: Standard YouTube License, CC-BY