Different disturbances—one pathway of protein unfolding. Actin folding-unfolding and misfolding

Authors

  • Olga I. Povarova,

    1. Laboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology Russian Academy of Science, Tikhoretsky Avenue, 4, St. Petersburg 194064, Russia
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  • Irina M. Kuznetsova,

    1. Laboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology Russian Academy of Science, Tikhoretsky Avenue, 4, St. Petersburg 194064, Russia
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  • Konstantin K. Turoverov

    Corresponding author
    1. Laboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology Russian Academy of Science, Tikhoretsky Avenue, 4, St. Petersburg 194064, Russia
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Corresponding author. Tel.: +7 812 297 1957; fax: +7 812 297 0341. kkt@mail.cytspb.rssi.ru

Abstract

This review summarizes the results of our investigations of actin unfolding-refolding and presents the notion that protein unfolding pathway, the number and the appearance order of intermediate states do not dependent on denaturing agents. To place our concept in the context of current knowledge of protein folding, we review in brief the development of general ideas of protein folding mechanisms, paying special attention to some key points of this process. Thus we focus on the characteristics of amino acid sequences that provide the existence of protein native structure, and on the interactions that compensate the increase of free energy due to the decrease of entropy on the way from multitude unfolded conformations to unique native state. In particular, we emphasize that ordered structures can arise both due to intramolecular and intermolecular interactions which lead to the formation of native and misfolded (associates, amorphous aggregates amyloid and amyloid-like fibrils) states, respectively.

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