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

In the context of protein folding, the burial of hydrophobic amino acid residues within the protein’s core is entropically driven by the release of

A. Covalently bound water molecules
B. Ordered water molecules from the clathrate cages around the exposed hydrophobic groups
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C. Calcium ions that were bridging water to the protein
D. Protons that were attached to the polar water molecules

📝 Explanation

Surrounding exposed non-polar groups, water forms highly ordered, low-entropy cages. When these groups aggregate in the protein's core, this caged water is released into the bulk solution, significantly increasing its entropy. This increase in the entropy of water is a major driving force for protein folding.

📖 Additional Information

  • Covalently bound water molecules
  • Ordered water molecules from the clathrate cages around the exposed hydrophobic groups
  • Calcium ions that were bridging water to the protein
  • Protons that were attached to the polar water molecules

Surrounding exposed non-polar groups, water forms highly ordered, low-entropy cages. When these groups aggregate in the protein's core, this caged water is released into the bulk solution, significantly increasing its entropy. This increase in the entropy of water is a major driving force for protein folding.

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