The Folding Process of Apomyoglobin

Marc      Jamin

doi:10.2174/0929866053587174

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

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Protein & Peptide Letters

Title: The Folding Process of Apomyoglobin

Volume: 12 Issue: 3

Author(s): Marc Jamin

Affiliation:

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

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.