Textbook Question
Myoglobin is a protein containing 153 amino acids. Approximately half of the amino acids in myoglobin have polar side chains.
b. Where would you expect the nonpolar side chains to be?
Ch.10 Proteins Workers of the Cell
Frost4th EditionGeneral, Organic and Biological ChemistryISBN: 9780134988696
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Table of contents
- Ch.4 Introduction to Organic Compounds75
- Ch.5 Chemical Reactions19
- Ch.6 Carbohydrates Life's Sweet Molecules62
- Ch.7 States of Matter and Their Attractive Forces8
- Ch.8 Solution Chemistry Sugar and Water Do Mix4
- Ch.10 Proteins Workers of the Cell89
- Ch.11 Nucleic Acids Big Molecules with a Big Role69
- Ch.12 Food as Fuel An Overview of Metabolism65
Frost4th EditionGeneral, Organic and Biological ChemistryISBN: 9780134988696Not the one you use?Change textbook
Chapter 6, Problem 35b
Identify each of the following statements as characteristic of protein denaturation or protein hydrolysis.
b. A protein breaks up into amino acid fragments.
Verified step by step guidance1
Understand the two processes: Protein denaturation refers to the disruption of a protein's secondary, tertiary, or quaternary structure without breaking peptide bonds, while protein hydrolysis involves breaking the peptide bonds, resulting in smaller fragments or individual amino acids.
Analyze the statement: 'A protein breaks up into amino acid fragments.' This indicates that the protein is being broken down into its building blocks, which are amino acids.
Recognize that breaking peptide bonds is a characteristic of protein hydrolysis, as this process cleaves the bonds between amino acids in the protein chain.
Conclude that the statement describes protein hydrolysis because it explicitly mentions the breakdown of the protein into amino acid fragments.
Remember that protein denaturation does not involve breaking peptide bonds but rather the unfolding or structural alteration of the protein.
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Key Concepts
Here are the essential concepts you must grasp in order to answer the question correctly.
Protein Denaturation
Protein denaturation refers to the process where a protein loses its native structure due to external factors such as heat, pH changes, or chemical agents. This alteration affects the protein's functionality but does not break the peptide bonds between amino acids. Denatured proteins may aggregate or unfold, leading to loss of biological activity.
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1:17
Digestion of Proteins Example 1
Protein Hydrolysis
Protein hydrolysis is a biochemical process where proteins are broken down into smaller peptides or amino acids through the addition of water. This reaction is typically catalyzed by enzymes or acids and involves the cleavage of peptide bonds. Hydrolysis is essential for digestion and the recycling of amino acids in the body.
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Peptide Bonds
Peptide bonds are the covalent bonds that link amino acids together to form proteins. These bonds are formed through a dehydration synthesis reaction, where a molecule of water is released. Understanding peptide bonds is crucial for distinguishing between processes like denaturation, which does not break these bonds, and hydrolysis, which specifically targets and cleaves them.
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Related Practice
Textbook Question
List the type of attractive force disrupted and the level of protein structure changed by the following denaturing treatments:
a. adding salt to soy milk to make tofu
Textbook Question
Identify each of the following statements as characteristic of protein denaturation or protein hydrolysis.
a. Milk curdles when lemon juice is added to it.
Textbook Question
Match each protein in column A with its function in column B:
Textbook Question
What is the name given to the reactant of an enzyme-catalyzed reaction?
Textbook Question
What is the name given to a small, organic nonprotein part of an enzyme that is involved in catalysis?