Protein folding and stability in the presence of osmolytes

被引:9
|
作者
Fonin A.V. [1 ]
Uversky V.N. [1 ,2 ]
Kuznetsova I.M. [1 ]
Turoverov K.K. [1 ,3 ]
机构
[1] Institute of Cytology, Russian Academy of Sciences, Tikhoretsky pr. 4, St. Petersburg
[2] Department of Molecular Medicine, College of Medicine, University of South Florida, 12901 Bruce B. Downs Blvd. MDC07, Tampa, 33612, FL
[3] St. Petersburg State Polytechnical University, Polytechnicheskaya ul. 29, St. Petersburg
关键词
denaturation; folding; osmolytes; osmotic stress; proteins; stability;
D O I
10.1134/S0006350916020056
中图分类号
学科分类号
摘要
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. © 2016, Pleiades Publishing, Inc.
引用
收藏
页码:185 / 192
页数:7
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