“…Subsequent conformational change, involving major reorganization of a large, exposed proteinaserecognition loop and one of the three  sheets, is fundamental to the normal functioning of many serpins as suicide inhibitors of serine and cysteine proteinases. Other properties of serpins, such as antiangiogenic activity (O'Reilly et al 1999), chemotactic response (Potempa et al 1991;Banda et al 1988;Hoffman et al 1989), or ability to regulate cell migration (Stefansson and Lawrence 1996) also appear to depend on the serpin's ability to undergo conformational change. The primary structure of a serpin must therefore ensure not only that a folding pathway leading to the metastable conformation be followed but that, under appropriate circumstances, structural rearrangement to the most stable state can occur rapidly and smoothly enough to carry out the physiological function of the serpin.…”