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<p>conformations because those conformers have lower energy than unfolded and mis-folded states (??G of folding). This is achieved by a distributed, internal network of cooperative interactions (<a href="page.php?w=hydrophobic">hydrophobic</a>, <a href="page.php?w=polarity_%28chemistry%29">polar</a> and <a href="page.php?w=covalent_bond">covalent</a>). Protein structural robustness results from few single mutations being sufficiently disruptive to compromise function. Proteins have also evolved to avoid <a href="page.php?w=protein_aggregation">aggregation</a></p><p>
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