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The Folding Process of Apomyoglobin

[ Vol. 12 , Issue. 3 ]

Author(s):

Marc Jamin   Pages 229 - 234 ( 6 )

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

Affiliation:

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



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