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<p>Some tertiary protein structures may exist in long-lived states that are not the expected most stable state. For example, many <a href="page.php?w=serpins">serpins</a> (serine protease inhibitors) show this <a href="page.php?w=metastability">metastability</a>. They undergo a <a href="page.php?w=conformational_change">conformational change</a> when a loop of the protein is cut by a <a href="page.php?w=protease">protease</a>.</p>

<p><big> Chaperone proteins </big></p>
<p>It is commonly assumed that the native state of a protein is also the most <a href="page.php?w=thermodynamics">thermodynamically</a></p><p>
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