BIO NMDCAT Biological Importance of Water
nmdcat.online June 27, 2026

The dissolution of a protein’s tertiary structure by a high concentration of urea is an example of the disruption of the hydrophobic effect, which is central to protein folding. The hydrophobic effect is driven by

A. The strong attraction between non-polar molecules for each other
B. The thermodynamic drive for water molecules to maximize their entropy by excluding non-polar groups
C. The formation of covalent bonds between the non-polar groups in the protein core
D. The ability of water to form hydrogen bonds with hydrophobic side chains

📝 Explanation

Water molecules form highly ordered "cage-like" structures around exposed non-polar groups, which decreases entropy. To minimize this, water forces non-polar groups to aggregate, freeing the caged water and increasing overall entropy. This entropic force is the hydrophobic effect.

📖 Additional Information

  • The strong attraction between non-polar molecules for each other
  • The thermodynamic drive for water molecules to maximize their entropy by excluding non-polar groups
  • The formation of covalent bonds between the non-polar groups in the protein core
  • The ability of water to form hydrogen bonds with hydrophobic side chains

Water molecules form highly ordered "cage-like" structures around exposed non-polar groups, which decreases entropy. To minimize this, water forces non-polar groups to aggregate, freeing the caged water and increasing overall entropy. This entropic force is the hydrophobic effect.

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