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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0:59 minutes

Problem 23

Textbook Question

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

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Understand that proteins have different levels of structure: primary, secondary, tertiary, and quaternary.

Recognize that secondary structures of proteins include alpha helices and beta sheets.

Identify that the stabilizing force in these secondary structures is due to interactions between the backbone atoms of the polypeptide chain.

Recall that the specific type of interaction responsible for stabilizing these structures is hydrogen bonding.

Conclude that hydrogen bonds form between the carbonyl oxygen of one amino acid and the amide hydrogen of another, stabilizing the secondary structure.

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Key Concepts

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

Hydrogen Bonds

Hydrogen bonds are weak attractions that occur between a hydrogen atom covalently bonded to an electronegative atom and another electronegative atom. In proteins, these bonds play a crucial role in stabilizing secondary structures such as alpha helices and beta sheets, contributing to the overall three-dimensional shape of the protein.

Secondary Structure

Secondary structure refers to the local folded structures that form within a protein due to interactions between the backbone atoms. The most common types are alpha helices and beta sheets, which are stabilized by hydrogen bonds. Understanding these structures is essential for grasping how proteins achieve their functional forms.

Protein Folding

Protein folding is the process by which a polypeptide chain acquires its functional three-dimensional shape. This process is driven by various interactions, including hydrogen bonds, hydrophobic interactions, and ionic bonds. Proper folding is critical for protein function, and misfolding can lead to diseases.