Table of contents

1. Matter and Measurements4h 31m
2. Atoms and the Periodic Table5h 23m
3. Ionic Compounds2h 18m
4. Molecular Compounds2h 18m
5. Classification & Balancing of Chemical Reactions3h 17m
6. Chemical Reactions & Quantities2h 27m
7. Energy, Rate and Equilibrium3h 46m
8. Gases, Liquids and Solids3h 25m
9. Solutions4h 10m
10. Acids and Bases3h 29m
11. Nuclear Chemistry56m
BONUS: Lab Techniques and Procedures1h 38m
BONUS: Mathematical Operations and Functions47m
12. Introduction to Organic Chemistry1h 34m
13. Alkenes, Alkynes, and Aromatic Compounds2h 12m
14. Compounds with Oxygen or Sulfur1h 6m
15. Aldehydes and Ketones1h 1m
16. Carboxylic Acids and Their Derivatives1h 11m
17. Amines39m
18. Amino Acids and Proteins1h 51m
19. Enzymes1h 37m
20. Carbohydrates1h 41m
21. The Generation of Biochemical Energy2h 8m
22. Carbohydrate Metabolism2h 22m
23. Lipids2h 26m
24. Lipid Metabolism1h 45m
25. Protein and Amino Acid Metabolism1h 37m
26. Nucleic Acids and Protein Synthesis2h 54m

18. Amino Acids and Proteins

Secondary Protein Structure

GOB Chemistry

18. Amino Acids and Proteins

Secondary Protein Structure

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3:33 minutes

Problem 73c

Textbook Question

For each of the following proteins, note whether the main secondary structure feature is α helix, β-pleated sheet, or both.
c. hemoglobin

Verified step by step guidance

Understand the secondary structure of proteins: Proteins have secondary structures such as α helices and β-pleated sheets, which are stabilized by hydrogen bonding between the backbone atoms of the polypeptide chain.

Recall the structure of hemoglobin: Hemoglobin is a globular protein that functions as an oxygen carrier in the blood. It is composed of four polypeptide chains (two α chains and two β chains).

Identify the secondary structure of hemoglobin: Hemoglobin's polypeptide chains primarily consist of α helices as their main secondary structure feature.

Note the absence of β-pleated sheets: Hemoglobin does not have significant β-pleated sheet structures in its secondary structure.

Conclude that the main secondary structure feature of hemoglobin is the α helix.

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Key Concepts

Here are the essential concepts you must grasp in order to answer the question correctly.

Secondary Structure of Proteins

The secondary structure of proteins refers to the local folded structures that form within a polypeptide due to hydrogen bonding between backbone atoms. The two most common types are α helices, which are coiled structures, and β-pleated sheets, which are formed by parallel or antiparallel strands. Understanding these structures is crucial for analyzing protein function and stability.

Hemoglobin Structure

Hemoglobin is a globular protein found in red blood cells, responsible for transporting oxygen. Its structure includes both α helices and β-pleated sheets, contributing to its functionality and stability. The presence of these secondary structures allows hemoglobin to undergo conformational changes necessary for oxygen binding and release.

Protein Folding and Function

Protein folding is the process by which a polypeptide chain acquires its functional three-dimensional structure. The specific arrangement of secondary structures, such as α helices and β-pleated sheets, plays a critical role in determining the overall shape and function of the protein. Misfolding can lead to loss of function or diseases, highlighting the importance of understanding these structural features.

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What are some differences between each of the following pairs?

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Name the stabilizing attractive force found in secondary structures of proteins.

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For each of the following proteins, note whether the main secondary structure feature is α helix, β-pleated sheet, or both.

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For each of the following proteins, note whether the main secondary structure feature is α helix, β-pleated sheet, or both.

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Globular proteins are water-soluble, whereas fibrous proteins are insoluble in water. Indicate whether you expect the following amino acids to be on the surface of a globular protein or on the surface of a fibrous protein.

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What is meant by the following terms as they apply to protein structure, and what bonds or molecular interactions stabilize that level of structure?

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