Textbook Question
How do the following interactions help to stabilize the tertiary and quaternary structure of a protein? Give an example of a pair of amino acids that could give rise to each interaction.
b. Disulfide bonds
Ch.18 Amino Acids and Proteins
McMurry8th EditionFundamentals of General, Organic, and Biological ChemistryISBN: 9780134015187
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Table of contents
- Ch.1 Matter and Measurements27
- Ch.2 Atoms and the Periodic Table20
- Ch.3 Ionic Compounds8
- Ch.4 Molecular Compounds23
- Ch.5 Classification & Balancing of Chemical Reactions12
- Ch.6 Chemical Reactions: Mole and Mass Relationships28
- Ch.7 Chemical Reactions: Energy, Rate and Equilibrium64
- Ch.8 Gases, Liquids and Solids24
- Ch.9 Solutions52
- Ch.10 Acids and Bases25
- Ch.11 Nuclear Chemistry22
- Ch.12 Introduction to Organic Chemistry: Alkanes57
- Ch.13 Alkenes, Alkynes, and Aromatic Compounds47
- Ch.14 Some Compounds with Oxygen, Sulfur, or a Halogen50
- Ch.15 Aldehydes and Ketones45
- Ch.16 Amines42
- Ch.17 Carboxylic Acids and Their Derivatives57
- Ch.18 Amino Acids and Proteins82
- Ch.19 Enzymes and Vitamins63
- Ch.20 Carbohydrates44
- Ch.21 The Generation of Biochemical Energy65
- Ch.22 Carbohydrate Metabolism45
- Ch.23 Lipids42
- Ch.24 Lipid Metabolism33
- Ch.25 Protein and Amino Acid Metabolism24
- Ch.26 Nucleic Acids and Protein Synthesis45
McMurry8th EditionFundamentals of General, Organic, and Biological ChemistryISBN: 9780134015187Not the one you use?Change textbook
Chapter 18, Problem 93a
Explain how a protein is denatured by the following:
a. Heat
Verified step by step guidance1
Understand the concept of protein denaturation: Denaturation is the process by which a protein loses its native three-dimensional structure due to the disruption of non-covalent interactions (e.g., hydrogen bonds, ionic bonds, hydrophobic interactions) and sometimes covalent bonds (e.g., disulfide bridges). This process does not break peptide bonds, so the primary structure remains intact.
Recognize the role of heat in denaturation: Heat provides energy that disrupts the weak non-covalent interactions holding the protein's secondary, tertiary, and quaternary structures together. These interactions are sensitive to temperature changes.
Describe the mechanism of heat-induced denaturation: As the temperature increases, the kinetic energy of the protein molecules increases. This causes the molecules to vibrate more vigorously, breaking hydrogen bonds and other stabilizing interactions. This leads to the unfolding of the protein's structure.
Explain the consequences of denaturation: When the protein unfolds, it loses its specific shape, which is critical for its biological function. This loss of structure results in the loss of the protein's activity.
Provide an example: For instance, when an egg is cooked, the heat denatures the proteins in the egg white (mainly albumin), causing them to unfold and aggregate, which changes the egg white from a clear liquid to a solid white mass.
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Key Concepts
Here are the essential concepts you must grasp in order to answer the question correctly.
Protein Structure
Proteins are composed of long chains of amino acids that fold into specific three-dimensional shapes. This structure is crucial for their function and is organized into four levels: primary (amino acid sequence), secondary (alpha helices and beta sheets), tertiary (overall 3D shape), and quaternary (multiple polypeptide chains). Understanding these levels is essential to grasp how denaturation affects protein functionality.
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3:26
Quaternary Protein Structure Concept 1
Denaturation
Denaturation refers to the process where proteins lose their native structure due to external stressors, such as heat, pH changes, or chemicals. This alteration disrupts the non-covalent interactions (like hydrogen bonds and hydrophobic interactions) that maintain the protein's shape, leading to a loss of biological activity. Denatured proteins may aggregate or precipitate, further impacting their function.
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1:17Digestion of Proteins Example 1
Effects of Heat on Proteins
Heat can cause proteins to denature by increasing molecular motion, which disrupts the weak interactions holding the protein's structure together. As temperature rises, the kinetic energy of the molecules increases, leading to the unfolding of the protein. This process is often irreversible, meaning that once a protein is denatured by heat, it may not regain its original structure or function.
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02:19Heat Capacity
Related Practice
Textbook Question
Give an example of a protein that has quaternary structure. How many polypeptide chains are present in this protein?
Textbook Question
How do the following noncovalent interactions help to stabilize the tertiary and quaternary structure of a protein? Give an example of a pair of amino acids that could give rise to each interaction.
a. Hydrophobic interactions
Textbook Question
Fresh pineapple cannot be used in gelatin desserts because it contains an enzyme that hydrolyzes the proteins in gelatin, destroying the gelling action. Canned pineapple can be added to gelatin with no problem. Why?
Textbook Question
Explain how a protein is denatured by the following:
c. Organic solvents
Textbook Question
Explain how a protein is denatured by the following:
b. Strong acids