hard · MCAT chem-phys
Protein folding is often described as a spontaneous process (Δ G < 0) even though it results in a more ordered protein structure (reduced protein entropy).
What explains this thermodynamic favorability?
- The increase in entropy of the surrounding water molecules due to the hydrophobic effect.
- The process is actually non-spontaneous overall and requires ATP-driven chaperones throughout.
- The decrease in enthalpy (Δ H < 0) from breaking hydrogen bonds between protein and water.
- New strong covalent peptide bonds form continuously throughout the entire folding process.
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