Hydrophobic Effect quiz #1 Flashcards
Hydrophobic Effect quiz #1
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What is the hydrophobic effect and why is it important in biological systems?
The hydrophobic effect is the exclusion of hydrophobic (water-fearing) substances by water, causing them to clump together and form separate phases. It is crucial for processes like protein folding and membrane formation in biological systems. Why do hydrophobic molecules clump together in water if they do not have a strong attraction for each other?
Hydrophobic molecules clump together in water not because of a strong attraction between them, but because clumping reduces the number of water molecules in hydration shells, allowing those water molecules to break free and increase the overall entropy of the universe, making the process thermodynamically favorable. How does the formation of hydration shells around nonpolar substances affect the entropy of water molecules?
The formation of hydration shells around nonpolar substances causes water molecules to become more ordered and less able to participate in normal hydrogen bonding, which decreases their entropy. Explain how the hydrophobic effect contributes to protein folding.
During protein folding, nonpolar R groups clump together due to the hydrophobic effect, which releases water molecules from hydration shells and increases universal entropy, making the folding process thermodynamically favorable. Describe the role of the hydrophobic effect in membrane formation.
The hydrophobic effect causes the nonpolar tails of phospholipids to clump together, reducing hydration shells and releasing water molecules, which increases universal entropy and leads to the formation of a phospholipid bilayer. What happens to the entropy of the system and the universe when nonpolar substances clump together in water?
When nonpolar substances clump together in water, local entropy decreases, but the release of water molecules from hydration shells increases the entropy of the universe, making the overall process thermodynamically favorable. Why is the hydrophobic effect considered thermodynamically favorable despite decreasing local entropy?
The hydrophobic effect is thermodynamically favorable because the increase in universal entropy from the release of water molecules outweighs the decrease in local entropy caused by the clumping of nonpolar substances. What is the hydrophobic effect and why is it important in biological systems?
The hydrophobic effect is the exclusion of hydrophobic substances by water, causing them to clump together and form separate phases. It is crucial for processes like protein folding and membrane formation in biological systems. Why do hydrophobic molecules clump together in water if they do not have a strong attraction for each other?
Hydrophobic molecules clump together in water not because of a strong attraction between them, but because clumping reduces the number of water molecules in hydration shells, allowing those water molecules to break free and increase the overall entropy of the universe, making the process thermodynamically favorable. How does the formation of hydration shells around nonpolar substances affect the entropy of water molecules?
The formation of hydration shells around nonpolar substances causes water molecules to become more ordered and less able to participate in normal hydrogen bonding, which decreases their entropy.
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