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<p>bonding, van der Waals forces and Coloumb interactions. During folding, the number hydrophobic side-chains exposed to water is minimized, which is known as hydrophobic collapse, causing them to collapse into the core of the protein. This causes most globular proteins to have hydrophilic side-chains outwards on the surface exposed to solvent and hydrophobic side-chains in the core.</p>

<p><big> Protein stability </big></p>
<p>Thermodynamic stability of proteins represents the <a href="page.php?w=Gibbs_free_energy">free energy difference</a> between the</p><p>
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