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Dissociative mechanism for irreversible thermal denaturation of oligomeric proteins

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Abstract

Protein stability is a fundamental characteristic essential for understanding conformational transformations of the proteins in the cell. When using protein preparations in biotechnology and biomedicine, the problem of protein stability is of great importance. The kinetics of denaturation of oligomeric proteins may have characteristic properties determined by the quaternary structure. The kinetic schemes of denaturation can include the multiple stages of conformational transitions in the protein oligomer and stages of reversible dissociation of the oligomer. In this case, the shape of the kinetic curve of denaturation or the shape of the melting curve registered by differential scanning calorimetry can vary with varying the protein concentration. The experimental data illustrating dissociative mechanism for irreversible thermal denaturation of oligomeric proteins have been summarized in the present review. The use of test systems based on thermal aggregation of oligomeric proteins for screening of agents possessing anti-aggregation activity is discussed.

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Acknowledgments

We are very glad to congratulate Prof. Donald Winzor warmly on his 80th birthday. We wish him good health, many happy years of scientific activity and friendship of his many friends the world over. We appreciate greatly all that he has done to advance our understanding on the way macromolecules behave in the non-ideal environment. Since our review is devoted to the behavior of dissociating enzymes, it is relevant to remember that Prof. Donald Winzor and his colleagues were among those who started to elaborate the theory of allosteric regulation based on the displacement of the equilibrium between oligomeric enzyme forms under the influence of allosteric effectors (Frieden 1967; Kurganov 1967; Nichol et al. 1967). Further investigations of Prof. Donald Winzor concerning the role of the protein isomerization induced by the binding of specific ligands or the presence of small inert cosolutes in fulfillment of the biological functions of proteins were of great interest to us, and we were glad to carry out the joint study of the effects of crowding on the allosteric properties of glycogen phosphorylase b (Chebotareva et al. 2001, 2005). It was a very exciting experience for me (N.A.C.) to talk to Prof. Donald Winzor and to discuss out experimental results.

This study was supported by the Russian Science Foundation (grant 16-14-10055).

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  1. Bach Institute of Biochemistry, Research Center of Biotechnology of the Russian Academy of Sciences, Leninsky pr. 33, Moscow, 119071, Russia

    Natalia A. Chebotareva, Svetlana G. Roman & Boris I. Kurganov

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  1. Natalia A. Chebotareva
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  2. Svetlana G. Roman
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  3. Boris I. Kurganov
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Correspondence to Natalia A. Chebotareva.

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This article is part of a Special Issue on ‘Analytical Quantitative Relations in Biochemistry’ edited by Damien Hall and Stephen Harding.

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Chebotareva, N.A., Roman, S.G. & Kurganov, B.I. Dissociative mechanism for irreversible thermal denaturation of oligomeric proteins. Biophys Rev 8, 397–407 (2016). https://doi.org/10.1007/s12551-016-0220-z

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