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

Summary of Protein Structure

GOB Chemistry

18. Amino Acids and Proteins

Summary of Protein Structure

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3:42 minutes

Problem 71b

Textbook Question

Identify the level of protein structure associated with each of the following:
b. hydrogen bonding between backbone atoms

Verified step by step guidance

Understand the four levels of protein structure: primary, secondary, tertiary, and quaternary. Each level describes a different aspect of the protein's organization.

Recall that the primary structure refers to the sequence of amino acids in the polypeptide chain, held together by peptide bonds.

Recognize that the secondary structure involves local folding of the polypeptide chain into structures such as alpha-helices and beta-pleated sheets. These structures are stabilized by hydrogen bonding between backbone atoms (specifically, between the carbonyl oxygen of one amino acid and the amide hydrogen of another).

Note that tertiary structure refers to the overall three-dimensional shape of a single polypeptide chain, stabilized by interactions such as hydrogen bonds, ionic bonds, hydrophobic interactions, and disulfide bridges, but these involve side chains rather than backbone atoms.

Conclude that the level of protein structure associated with hydrogen bonding between backbone atoms is the secondary structure.

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Key Concepts

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

Protein Structure Levels

Proteins have four levels of structure: primary, secondary, tertiary, and quaternary. Each level represents a different aspect of protein organization, from the sequence of amino acids (primary) to the overall three-dimensional shape (tertiary) and the assembly of multiple polypeptide chains (quaternary). Understanding these levels is crucial for analyzing protein function and stability.

Secondary Structure

The secondary structure of a protein refers to local folded structures that form within a polypeptide due to hydrogen bonding between backbone atoms. Common examples include alpha helices and beta sheets. These structures are essential for the overall stability and functionality of proteins, as they contribute to the protein's three-dimensional conformation.

Hydrogen Bonding

Hydrogen bonding is a type of weak chemical bond that occurs when a hydrogen atom covalently bonded to an electronegative atom, like oxygen or nitrogen, interacts with another electronegative atom. In proteins, these bonds are critical for stabilizing secondary structures, as they help maintain the shape and integrity of the protein by linking different parts of the polypeptide chain.