Textbook Question
What kind of bond would you expect between the side chains of the following amino acids?
c. Aspartic acid and asparagine
Ch.18 Amino Acids and Proteins
McMurry8th EditionFundamentals of GOBISBN: 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
Chapter 18, Problem 84b
What is meant by the following terms as they apply to protein structure, and what bonds or molecular interactions stabilize that level of structure?
b. Secondary structure
Verified step by step guidance1
Understand that the secondary structure of a protein refers to the local folding of the polypeptide chain into specific patterns, such as alpha-helices and beta-pleated sheets. These structures are stabilized by hydrogen bonds between the backbone amide hydrogen (N-H) and carbonyl oxygen (C=O) groups of the polypeptide chain.
Recognize that alpha-helices are coiled structures where the hydrogen bonds form between the carbonyl oxygen of one amino acid and the amide hydrogen of an amino acid four residues away. This creates a helical shape.
Identify that beta-pleated sheets consist of strands of polypeptides lying side by side, which can be parallel or antiparallel. Hydrogen bonds form between the carbonyl oxygen of one strand and the amide hydrogen of another strand, stabilizing the sheet-like structure.
Note that secondary structures do not involve interactions between the side chains (R groups) of amino acids; they are solely dependent on the backbone interactions.
Understand that the stability of secondary structures is influenced by the sequence of amino acids, as certain residues (e.g., proline) can disrupt these structures due to their unique properties.
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Key Concepts
Here are the essential concepts you must grasp in order to answer the question correctly.
Secondary Structure
Secondary structure refers to the local folding patterns of a protein, primarily stabilized by hydrogen bonds between the backbone amide and carbonyl groups. The most common forms of secondary structure are alpha helices and beta sheets, which contribute to the overall shape and stability of the protein. These structures are crucial for the protein's function, as they create specific spatial arrangements that facilitate interactions with other molecules.
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1:24
Secondary Protein Structure Example 2
Hydrogen Bonds
Hydrogen bonds are weak interactions that occur when a hydrogen atom covalently bonded to an electronegative atom, like oxygen or nitrogen, is attracted to another electronegative atom. In the context of secondary structure, these bonds form between the carbonyl oxygen of one amino acid and the amide hydrogen of another, helping to stabilize the helical or sheet formations. Although individually weak, the cumulative effect of many hydrogen bonds significantly contributes to the stability of protein structures.
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Protein Folding
Protein folding is the process by which a linear chain of amino acids acquires its functional three-dimensional structure. This process is driven by various interactions, including hydrogen bonds, hydrophobic interactions, and van der Waals forces. Proper folding is essential for protein functionality, as misfolded proteins can lead to loss of function or diseases, highlighting the importance of secondary structure in the overall stability and activity of proteins.
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Related Practice
Textbook Question
Is the bond formed between each pair in Problem 18.76 covalent or noncovalent?
a. Cysteine and cysteine
b. Alanine and leucine
c. Aspartic acid and asparagine
d. Serine and lysine
Textbook Question
What is meant by the following terms as they apply to protein structure, and what bonds or molecular interactions stabilize that level of structure?
a. Primary structure
Textbook Question
What is meant by the following terms as they apply to protein structure, and what bonds or molecular interactions stabilize that level of structure?
d. Quaternary structure
Textbook Question
What level of protein structure is determined by the following:
a. Peptide bonds between amino acids?
Textbook Question
What level of protein structure is determined by the following:
b. Hydrogen bonds between backbone carbonyl oxygen atoms and hydrogen atoms attached to backbone nitrogen atoms?