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Biophys J, November 1999, p. 2788-2800, Vol. 77, No. 5

Effect of Self-Association on the Structural Organization of Partially Folded Proteins: Inactivated Actin

Irina M. Kuznetsova,* Alexander G. Biktashev,* Sofia Yu. Khaitlina,* Konstantin S. Vassilenko,# Konstantin K. Turoverov,* and Vladimir N. Uversky§

 *Institute of Cytology, Russian Academy of Sciences, 194064 St. Petersburg, Russia;  #Institute of Protein Research, Russian Academy of Sciences, Moscow Region, Russia;  §Institute for Biological Instrumentation, Russian Academy of Sciences, Moscow Region, Russia; and  Department of Chemistry and Biochemistry, University of California, Santa Cruz, California 95064 USA

The propensity to associate or aggregate is one of the characteristic properties of many nonnative proteins. The aggregation of proteins is responsible for a number of human diseases and is a significant problem in biotechnology. Despite this, little is currently known about the effect of self-association on the structural properties and conformational stability of partially folded protein molecules. G-actin is shown to form equilibrium unfolding intermediate in the vicinity of 1.5 M guanidinium chloride (GdmCl). Refolding from the GdmCl unfolded state is terminated at the stage of formation of the same intermediate state. An analogous form, known as inactivated actin, can be obtained by heat treatment, or at moderate urea concentration, or by the release of Ca2+. In all cases actin forms specific associates comprising partially folded protein molecules. The structural properties and conformational stability of inactivated actin were studied over a wide range of protein concentrations, and it was established that the process of self-association is rather specific. We have also shown that inactivated actin, being denatured, is characterized by a relatively rigid microenvironment of aromatic residues and exhibits a considerable limitation in the internal mobility of tryptophans. This means that specific self-association can play an important structure-forming role for the partially folded protein molecules.

Biophys J, November 1999, p. 2788-2800, Vol. 77, No. 5
© 1999 by the Biophysical Society   0006-3495/99/11/2788/13  $2.00


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