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 5, Problem 13TYK
What happens when a protein denatures?
- a. Its primary structure is disrupted.
- b. Its secondary and tertiary structures are disrupted.
- c. It flips inside out.
- d. Its hydrogen bonds, ionic bonds, hydrophobic interactions, disulfide bridges, and peptide bonds are disrupted.
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Describe the levels of structure of a protein and tell how they would be affected by: a. Hydrolysis with 6M HCl (breaks peptide bond)b. Heating with mercaptoethanol (breaks hydrogen bonds)
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Chapter 5 Solutions
Study Guide for Campbell Biology
Ch. 5 - Monomers are linked into polymers by ________...Ch. 5 - You can recognize a monosaccharide by its multiple...Ch. 5 - Number the carbons in the following glucose and...Ch. 5 - Prob. 4IQCh. 5 - Fill in this concept map to help you organize your...Ch. 5 - a. Draw the amino acids alanine (R group: CH3) and...Ch. 5 - In the following diagram of a portion of a...Ch. 5 - Now that you have gained experience with concept...Ch. 5 - a. Label the three parts of this nucleotide....Ch. 5 - Take the time to create a concept map that...
Ch. 5 - Prob. 1SYKCh. 5 - Prob. 2SYKCh. 5 - glycogen A. carbohydrate B. lipid C. protein D....Ch. 5 - cholesterol A. carbohydrate B. lipid C. protein D....Ch. 5 - RNA A. carbohydrate B. lipid C. protein D. nucleic...Ch. 5 - collagen A. carbohydrate B. lipid C. protein D....Ch. 5 - hemoglobin A. carbohydrate B. lipid C. protein D....Ch. 5 - A. carbohydrate B. lipid C. protein D. nucleic...Ch. 5 - Prob. 7TYKMCh. 5 - enzyme A. carbohydrate B. lipid C. protein D....Ch. 5 - cellulose A. carbohydrate B. lipid C. protein D....Ch. 5 - Chitin A. carbohydrate B. lipid C. protein D....Ch. 5 - Polymerization (the formation of polymers) is a...Ch. 5 - Which of the following statements is not true of a...Ch. 5 - Prob. 3TYKCh. 5 - Prob. 4TYKCh. 5 - Prob. 5TYKCh. 5 - Prob. 6TYKCh. 5 - A fatty acid that has the formula C16H32O2 is a....Ch. 5 - Prob. 8TYKCh. 5 - Prob. 9TYKCh. 5 - Prob. 10TYKCh. 5 - Which of the following molecules provides the most...Ch. 5 - Prob. 12TYKCh. 5 - What happens when a protein denatures? a. Its...Ch. 5 - The helix of proteins is a. part of a proteins...Ch. 5 - What is the best description of the following...Ch. 5 - Prob. 16TYKCh. 5 - Prob. 17TYKCh. 5 - Which of the following is true of the subunits of...Ch. 5 - Prob. 19TYKCh. 5 - If the nucleotide sequence of one strand of a DNA...Ch. 5 - How are nucleotide monomers connected to form a...Ch. 5 - Prob. 22TYK
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- Describe the four levels of protein structure. How do a proteins side groups influence its interactions with other substances? What happens when a protein is denatured?arrow_forwardHow would adding acid to a non-buffered solution be most likely to affect protein structure? Select one: a. Adding acid would disrupt the primary structure of the protein b. Adding acid would cause the protein to become a lipid c. Adding acid would cause the protein to become a carbohydrate d. Adding acid would disrupt the secondary and tertiary structure of the proteinarrow_forwardWhich of the following statements about amino acids is true? A. Twenty two amino acids are commonly found in proteins. B. Amino acids are often linked together to form branched polymers. C. All amino acids contain an NH2 and a COOH group. D. Most of the amino acids used in protein biosynthesis have charged side chains.arrow_forward
- How does the coplanar nature of the peptide bond impact the overall structure of a protein? O a. It facilitates the stacking of aromatic side chains. O b. It promotes the flexibility of the protein backbone. Oc. It restricts the formation of secondary structures. Od. It allows for the easy formation of disulfide bonds. It constrains the rotation around the peptide bond, influencing protein folding.arrow_forwardAt what level of protein structure does each of the following denaturation act? a. heat b. strong acid c. saturated salt solution d. organic solvents (e.g., alcohol or chloroform)arrow_forwardWhat is the general characteristic of protein domains? A. All protein domains exhibit both a and B structures B. Protein domains constitute supersecondary structures that have specific biological functions in proteins. C. Most protein domains can be hydrolyzed from parent polypeptide chains while retaining functions and/or structures that are conserved. D. Protein domains constitute the structural block from which the protein is built E. Protein domains contain motifs that are the binding sites for prosthetic groups such as heme, or the iron-sulfur clusters.arrow_forward
- Match the level of protein structure to its description: Primary Secondary Tertiary Quaternary A. Folding due to interactions among the peptide backbone B. Interactions among multiple polypeptide chains C. Sequence of amino acids D. Folding due to interactions among side chainsarrow_forwardWhich of the following statement about quaternary structure of protein is correct? Select one: a. Quaternary structure is a force between different polypeptides. b. Hydrogen bond is an only force found in quaternary structure. c. Quaternary structure contains one polypeptide. d. Quaternary structure is an unfolded form of protein.arrow_forwardThe difference between a polypeptide and a protein is a. that proteins are polypeptides folded up into a functional three-dimensional conformation b. that proteins are precursors of polypeptides c. that polypeptides are made of protein folded up into a functional three-dimensional conformation d. that proteins are always made with many polypeptidesarrow_forward
- which is true when speaking about the secondary structure of a protein A. invoves R group binding b. involves binding to other protiens c. involves hydrogen bonding of the protien backbone d. involves peptide bindingarrow_forwardWhich of the following statements are correct about the native state of a protein (select all that apply)? A. Polar sidechains commonly interact with water B. Hydrophobic amino acids tend to be on surface of protein C. The sidechains of polar amino acids are most commonly found in the central core of a protein D. Formation of an alpha-helix is primarily driven by hydrogen bonds between the protein main chain, not sidechains. E. Secondary structure is largely driven by hydrophobic interactionsarrow_forwardWhat type of bonding is present in the primary structure of proteins? A. peptide bond B. hydrogen bond C. ionic bond D. more than one choice is correctarrow_forward
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