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 group of amino acids is most likely to be present at the dimerization interface of STAT3 proteins?

Polar uncharged amino acids such as serine and threonine

Positively charged amino acids such as lysine and arginine

Negatively charged amino acids such as aspartate and glutamate

Hydrophobic amino acids such as leucine, isoleucine, and valine

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Verified step by step guidance

Understand the concept of protein dimerization: Protein dimerization often involves interactions between hydrophobic regions of the proteins. Hydrophobic amino acids tend to cluster together to minimize their exposure to water, stabilizing the dimer interface.

Review the properties of amino acid side chains: Hydrophobic amino acids, such as leucine, isoleucine, and valine, have nonpolar side chains that are ideal for forming hydrophobic interactions. These interactions are crucial for stabilizing the dimerization interface.

Eliminate other options based on their chemical properties: Polar uncharged amino acids (e.g., serine and threonine) are more likely to form hydrogen bonds, positively charged amino acids (e.g., lysine and arginine) interact with negatively charged groups, and negatively charged amino acids (e.g., aspartate and glutamate) interact with positively charged groups. None of these are primarily involved in hydrophobic interactions.

Relate the hydrophobic amino acids to the dimerization interface: Hydrophobic amino acids are typically found in the interior of protein structures or at interfaces where water exclusion is favorable, such as the dimerization interface of STAT3 proteins.

Conclude that hydrophobic amino acids are most likely to be present at the dimerization interface of STAT3 proteins, as their properties align with the requirements for stabilizing such interfaces through hydrophobic interactions.