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As with all proteins, the structural behavior of α 1 -antitrypsin determines its function. However, the functional mechanism by which α 1 -antitrypsin inhibits its target proteases is unusually dynamic, relating to its folding and the potential for it to adopt more thermodynamically stable forms than its native conformation. Alpha1-antitrypsin deficiency arises most commonly as a result of point mutations that affect the structure and dynamic behavior of α 1 -antitrypsin in solution during and after folding. Understanding the dynamic structural behavior of α 1 -antitrypsin, therefore, explains both how it functions in health and how it drives disease. Consequently, it identifies novel therapeutic strategies to treat the underlying pathogenic mechanisms in α 1 -antitrypsin deficiency.