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The Folding Process of Apomyoglobin

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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; folding kinetics; molten globule; protein folding

Document Type: Review Article


Affiliations: Laboratoire de Biophysique Moleculaire et Cellulaire, Universite Joseph Fourier, DRDC/BMC, 17 rue des Martyrs, 38054, Grenoble cedex 09, France.

Publication date: 2005-04-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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