Textbook Question
As a chef, you prepare a wide variety of foods daily. The following dishes all contain protein. What method (if any) has been used to denature the protein present in each food?
a. Charcoal-grilled steak
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 93c
Explain how a protein is denatured by the following:
c. Organic solvents
Verified step by step guidance1
Understand the concept of protein denaturation: Denaturation is the process in which a protein loses its native three-dimensional structure due to the disruption of non-covalent interactions, such as hydrogen bonds, ionic bonds, and hydrophobic interactions. This process does not break peptide bonds but alters the protein's functional shape.
Recognize the role of organic solvents: Organic solvents, such as ethanol or acetone, are capable of disrupting the hydrophobic interactions within a protein. These interactions are critical for maintaining the protein's tertiary structure, as hydrophobic side chains are typically buried in the interior of the protein to avoid contact with water.
Explain the mechanism of disruption: Organic solvents reduce the polarity of the surrounding environment, making it less favorable for hydrophobic side chains to remain buried. This causes the hydrophobic regions of the protein to unfold and become exposed to the solvent, leading to a loss of the protein's native structure.
Consider the impact on hydrogen bonding: Organic solvents can also interfere with hydrogen bonding by competing with water molecules or directly interacting with polar groups in the protein. This further destabilizes the protein's secondary and tertiary structures.
Summarize the result: The combined effects of disrupted hydrophobic interactions and hydrogen bonding lead to the unfolding of the protein, rendering it non-functional. This process is reversible or irreversible depending on the specific protein and conditions.
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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 structures. These structures are crucial for their function and are categorized into four levels: primary, secondary, tertiary, and quaternary. The stability of these structures is maintained by various interactions, including hydrogen bonds, ionic bonds, and hydrophobic interactions.
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Quaternary Protein Structure Concept 1
Denaturation
Denaturation refers to the process where a protein loses its native structure due to external stressors, such as heat, pH changes, or chemical agents. This alteration disrupts the interactions that maintain the protein's shape, leading to a loss of function. Denatured proteins may aggregate or precipitate, rendering them biologically inactive.
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Organic Solvents
Organic solvents, such as ethanol or acetone, can disrupt the hydrophobic interactions within proteins. These solvents can solvate nonpolar amino acid side chains, leading to the unfolding of the protein structure. The presence of organic solvents can also alter the protein's environment, further promoting denaturation and affecting its solubility and functionality.
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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
For each amino acid listed, tell whether its influence on tertiary structure is largely through hydrophobic interactions, hydrogen bonding, formation of salt bridges, covalent bonding, or some combination of these effects.
a. Tyrosine
Textbook Question
Explain how a protein is denatured by the following:
a. Heat
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:
b. Strong acids