Table of contents

1. Introduction to Biochemistry4h 34m
2. Water3h 23m
3. Amino Acids8h 10m
4. Protein Structure10h 4m
5. Protein Techniques14h 5m
6. Enzymes and Enzyme Kinetics13h 38m
7. Enzyme Inhibition and Regulation 8h 42m
8. Protein Function 9h 41m
9. Carbohydrates7h 49m
10. Lipids5h 49m
11. Biological Membranes and Transport 6h 37m
12. Biosignaling9h 45m
Review 1: Nucleic Acids, Lipids, & Membranes2h 47m
Review 2: Biosignaling, Glycolysis, Gluconeogenesis, & PP-Pathway3h 12m
Review 3: Pyruvate & Fatty Acid Oxidation, Citric Acid Cycle, & Glycogen Metabolism2h 26m
Review 4: Amino Acid Oxidation, Oxidative Phosphorylation, & Photophosphorylation1h 48m

3. Amino Acids

Amino Acid Groups

Biochemistry

3. Amino Acids

Amino Acid Groups

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Multiple Choice

Which type of amino acid R groups are most likely to line the interior of a channel protein that facilitates the passage of water-soluble molecules?

Polar and charged R groups

Aromatic R groups only

Nonpolar, hydrophobic R groups

Sulfur-containing R groups

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Verified step by step guidance

Understand the function of the channel protein: Channel proteins facilitate the passage of water-soluble molecules, which are typically polar or charged. This means the interior of the channel must interact favorably with these molecules.

Recall the properties of amino acid R groups: Amino acids have different R groups that can be polar, nonpolar, charged, aromatic, or sulfur-containing. Polar and charged R groups are hydrophilic, meaning they interact well with water and water-soluble molecules.

Consider the environment inside the channel: Since the channel's interior must accommodate water-soluble molecules, it is likely lined with amino acids that have polar or charged R groups to create a hydrophilic environment.

Eliminate incorrect options: Nonpolar, hydrophobic R groups would repel water-soluble molecules, aromatic R groups are not specifically suited for interacting with water, and sulfur-containing R groups are not inherently hydrophilic.

Conclude that polar and charged R groups are the most likely to line the interior of the channel protein, as they facilitate interactions with water-soluble molecules.