Abstract

Apomyoglobin (apoMb) folds through at least two partially folded forms that are detected both as transient intermediates during folding/unfolding kinetics or as stable intermediates at equilibrium. Here, I summarize the results of recent kinetic studies, which combined with detailed characterizations of equilibrium forms of the protein, provide a very detailed picture of apoMb folding process. The data are consistent with a linear U Ia Ib N model where compaction and structure are progressively acquired.

Keywords: apomyoglobin, protein folding, folding kinetics, molten globule