Protein folding and stability in the presence of osmolytes


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Abstract

Osmolytes are molecules whose function, among others, is to balance the hydrostatic pressure between the intracellular and extracellular compartments. Accumulation of osmolytes in a cell occurs in response to stress caused by changes in pressure, temperature, pH, or the concentration of inorganic salts. Osmolytes can prevent the denaturation of native proteins and promote the renaturation of unfolded proteins. Investigation of the roles of osmolyte in these processes is essential for our understanding of the mechanisms of protein folding and function in vivo. The large number of published reports that have been devoted to the effects of osmolytes on proteins are not always consistent with each other. In this review, an attempt is made to systemize the array of data on this subject and to consider the problem of protein folding and stability in osmolyte solutions from a single viewpoint.

About the authors

A. V. Fonin

Institute of Cytology

Author for correspondence.
Email: alexfonin@incras.ru
Russian Federation, Tikhoretsky pr. 4, St. Petersburg, 194064

V. N. Uversky

Institute of Cytology; Department of Molecular Medicine, College of Medicine

Email: alexfonin@incras.ru
Russian Federation, Tikhoretsky pr. 4, St. Petersburg, 194064; 12901 Bruce B. Downs Blvd. MDC07, Tampa, Florida, 33612

I. M. Kuznetsova

Institute of Cytology

Email: alexfonin@incras.ru
Russian Federation, Tikhoretsky pr. 4, St. Petersburg, 194064

K. K. Turoverov

Institute of Cytology; St. Petersburg State Polytechnical University

Email: alexfonin@incras.ru
Russian Federation, Tikhoretsky pr. 4, St. Petersburg, 194064; Polytechnicheskaya ul. 29, St. Petersburg, 195251

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