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

Where in a protein would you most likely find the R group (side chain) of a hydrophobic amino acid?

In the active site, forming hydrogen bonds with substrates

Buried in the interior of the protein, away from water

Exposed on the surface of the protein, interacting with water

Covalently bonded to a prosthetic group

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Verified step by step guidance

Understand the nature of hydrophobic amino acids: Hydrophobic amino acids have nonpolar side chains that do not interact favorably with water. Examples include leucine, isoleucine, valine, and phenylalanine.

Recall protein structure and folding principles: Proteins fold in a way that minimizes unfavorable interactions with the surrounding aqueous environment. Hydrophobic side chains tend to be buried in the interior of the protein to avoid contact with water.

Consider the environment of the active site: The active site of a protein often contains polar or charged residues to interact with substrates via hydrogen bonding or ionic interactions. Hydrophobic residues are less likely to be found here unless they are involved in specific substrate binding.

Evaluate the surface of the protein: The surface of a protein is typically exposed to water, so hydrophilic (polar or charged) amino acids are more likely to be found here, interacting with the aqueous environment.

Conclude based on the options provided: Hydrophobic amino acids are most likely to be buried in the interior of the protein, away from water, as this arrangement is energetically favorable and consistent with protein folding principles.