Apomyoglobin, myoglobin lacking the haem group, is a natural intermediate in biosynthesis of myoglobin, and has some structural features in common with the haem-containing native state. Unfolding or refolding studies of apomyoglobin have identified a molten globule intermediate at acid pH. We show here that both the native state of apomyoglobin and the molten globule intermediate have highly plastic structures. Substitution of single amino acids on the surface or in the interior of helices in the native protein produce dramatic changes in the helix content and tryptophan emission of apomyoglobin at neutral and acidic pH. The signals from the intermediate and native apomyoglobin correlate closely suggesting that apomyoglobin itself has a molten globule-like character, its structure representing a population of interconverting substates rather than a fixed conformation.
ASJC Scopus subject areas
- Structural Biology