The folding process of apomyoglobin.
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.
Jamin
Marc
M
Laboratoire de Biophysique Moléculaire et Cellulaire, Université Joseph Fourier, DRDC/BMC, 17 rue des Martyrs, 38054, Grenoble cedex 09, France. marc.jamin@UJF-grenoble.fr
D001059:Apoproteins / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D008958:Models, Molecular; D009211:Myoglobin / Q000737:chemistry*; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding
D001059:Apoproteins; D009211:Myoglobin; C010857:apomyoglobin