Textbook Question
What is the difference in hydrogen bonding between an α helix and a β−pleated sheet?
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Ch.16 Amino Acids, Proteins, and Enzymes
Timberlake13th EditionChemistry: An Introduction to General, Organic, and Biological ChemistryISBN: 9780134421353
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Table of contents
- Ch.1 Chemistry in Our Lives11
- Ch.2 Chemistry and Measurements80
- Ch.3 Matter and Energy54
- Ch.4 Atoms and Elements51
- Ch.5 Nuclear Chemistry42
- Ch.6 Ionic and Molecular Compounds57
- Ch.7 Chemical Quantities and Reactions41
- Ch.8 Gases29
- Ch.9 Solutions51
- Ch.10 Acids and Bases and Equilibrium65
- Ch.11 Introduction to Organic Chemistry: Hydrocarbons78
- Ch.12 Alcohols, Thiols, Ethers, Aldehydes, and Ketones83
- Ch.13 Carbohydrates54
- Ch.14 Carboxylic Acids, Esters, Amines, and Amides90
- Ch.15 Lipids61
- Ch.16 Amino Acids, Proteins, and Enzymes84
- Ch.17 Nucleic Acids and Protein Synthesis83
- Ch.18 Metabolic Pathways and ATP Production67
Timberlake13th EditionChemistry: An Introduction to General, Organic, and Biological ChemistryISBN: 9780134421353Not the one you use?Change textbook
Chapter 16, Problem 17
What happens when a primary structure forms a secondary structure?
Verified step by step guidance1
Understand the primary structure: The primary structure of a protein refers to the sequence of amino acids linked together by peptide bonds. This sequence determines the protein's properties and function.
Recognize the secondary structure: The secondary structure arises when the polypeptide chain folds or coils due to hydrogen bonding between the backbone atoms (not the side chains). Common secondary structures include alpha-helices and beta-pleated sheets.
Identify the role of hydrogen bonds: Hydrogen bonds form between the oxygen atom of the carbonyl group (C=O) and the hydrogen atom of the amine group (N-H) in the backbone. These bonds stabilize the secondary structure.
Examine the alpha-helix formation: In an alpha-helix, the polypeptide chain coils into a spiral shape, with hydrogen bonds forming between every fourth amino acid. This structure is compact and provides stability.
Explore the beta-pleated sheet formation: In a beta-pleated sheet, the polypeptide chains align side by side, forming hydrogen bonds between adjacent chains. These sheets can be parallel or antiparallel, depending on the direction of the chains.
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Key Concepts
Here are the essential concepts you must grasp in order to answer the question correctly.
Primary Structure
The primary structure of a protein refers to its unique sequence of amino acids, which are linked together by peptide bonds. This sequence is determined by the genetic code and dictates the protein's overall shape and function. Any changes in this sequence can lead to significant alterations in the protein's properties.
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1:11
Primary Protein Structure Example 1
Secondary Structure
Secondary structure refers to the local folded structures that form within a protein due to hydrogen bonding between the backbone atoms. Common types of secondary structures include alpha helices and beta sheets. These structures are crucial for the protein's stability and play a significant role in its overall three-dimensional conformation.
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1:24Secondary Protein Structure Example 2
Protein Folding
Protein folding is the process by which a protein achieves its functional three-dimensional shape from its linear primary structure. The formation of secondary structures is a key step in this process, as it helps stabilize the protein and allows for further folding into tertiary and quaternary structures. Proper folding is essential for the protein's biological activity.
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1:17Tertiary Protein Structure Example 1
Related Practice
Textbook Question
Peptides isolated from rapeseed that may lower blood pressure have the following sequence of amino acids. Draw the structure for each peptide and write the one-letter abbreviations.
a. Arg–Ile–Tyr
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Textbook Question
What type of interaction would you expect between the R groups of the following amino acids in a quaternary structure?
a. phenylalanine and isoleucine
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Textbook Question
What type of interaction would you expect between the R groups of the following amino acids in a tertiary structure?
c. serine and aspartate
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Textbook Question
Explain why each of the following pairs are complementary proteins:
a. beans and oats
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Textbook Question
Peptides from sweet potato with antioxidant properties have the following sequence of amino acids. Draw the structure for each peptide and write the one-letter abbreviations.
b. Asn–Tyr–Asp–Glu–Tyr
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