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Protein tertiary structure
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==== Metastability ==== Some tertiary protein structures may exist in long-lived states that are not the expected most stable state. For example, many [[serpins]] (serine protease inhibitors) show this [[metastability]]. They undergo a [[conformational change]] when a loop of the protein is cut by a [[protease]].<ref name="whis">{{cite journal | author = Whisstock J | year = 2006 | title = Molecular gymnastics: serpiginous structure, folding and scaffolding | journal = Current Opinion in Structural Biology | volume = 16 | issue = 6| pages = 761β68 | pmid = 17079131 | doi=10.1016/j.sbi.2006.10.005}}</ref><ref>{{cite journal |author=Gettins PG |title=Serpin structure, mechanism, and function |journal=Chem Rev |volume=102 |issue=12 |pages=4751β804 |year=2002 |pmid=12475206 |doi=10.1021/cr010170 }}</ref><ref>{{cite journal |vauthors=Whisstock JC, Skinner R, Carrell RW, Lesk AM |title=Conformational changes in serpins: I. The native and cleaved conformations of alpha(1)-anti-trypsin |pmid=10669617|journal=J Mol Biol |year=2000 |volume=296 |pages=685β99 |doi=10.1006/jmbi.1999.3520 |issue=2}}</ref>
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