Dissociative mechanism for irreversible thermal denaturation of oligomeric proteins

被引：17
作者：
Chebotareva N.A. [1 ]
Roman S.G. [1 ]
Kurganov B.I. [1 ]
机构：
[1] Bach Institute of Biochemistry, Research Center of Biotechnology of the Russian Academy of Sciences, Leninsky pr. 33, Moscow
来源：
Biophysical Reviews | 2016年 / 8卷 / 4期
基金：
俄罗斯科学基金会;
关键词：
Conformational lock; Dissociative mechanism; Oligomeric proteins; Protein denaturation;
D O I：
10.1007/s12551-016-0220-z
中图分类号：
学科分类号：
摘要：
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. © 2016, International Union for Pure and Applied Biophysics (IUPAB) and Springer-Verlag Berlin Heidelberg.
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页码：397 / 407
页数：10
相关论文
共 102 条
[11]  
Chebotareva N.A., Makeeva V.F., Bazhina S.G., Eronina T.B., Gusev N.B., Kurganov B.I., Interaction of Hsp27 with native phosphorylase kinase under crowding conditions, Macromol Biosci, 10, pp. 783-789, (2010)
[12]  
Chebotareva N.A., Eronina T.B., Roman S.G., Poliansky N.B., Muranov K.O., Kurganov B.I., Effect of crowding and chaperones on self-association, aggregation and reconstitution of apophosphorylase b, Int J Biol Macromol, 60, pp. 69-76, (2013)
[13]  
Chebotareva N.A., Eronina T.B., Sluchanko N.N., Kurganov B.I., Effect of Ca<sup>2+</sup> and Mg<sup>2+</sup> ions on oligomeric state and chaperone-like activity of αB-crystallin in crowded media, Int J Biol Macromol, 76, pp. 86-93, (2015)
[14]  
Chebotareva N.A., Filippov D.O., Kurganov B.I., Effect of crowding on several stages of protein aggregation in test systems in the presence of α-crystallin, Int J Biol Macromol, 80, pp. 358-365, (2015)
[15]  
Chukhrai E.S., Atyaksheva L.F., A physical chemistry view of the activity, stability, and adsorption properties of enzymes, Russ J Phys Chem A, 84, pp. 709-722, (2010)
[16]  
Curto L.M., Angelani C.R., Caramelo J.J., Delfino J.M., Truncation of a β-barrel scaffold dissociates intrinsic stability from its propensity to aggregation, Biophys J, 103, pp. 1929-1939, (2012)
[17]  
Davis-Searles P.R., Saunders A.J., Erie D.A., Winzor D.J., Pielak G.J., Interpreting the effect of small uncharged solutes on protein-folding equilibria, Annu Rev Biophys Biomol Struct, 30, pp. 271-306, (2001)
[18]  
Delahaije R.J., Wierenga P.A., Giuseppin M.L., Gruppen H., Comparison of heat-induced aggregation of globular proteins, J Agric Food Chem, 63, pp. 5257-5265, (2015)
[19]  
Ellis R.J., Macromolecular crowding: obvious but underappreciated, Trends Biochem Sci, 26, pp. 597-604, (2001)
[20]  
Ellis R.J., Minton A.P., Cell biology: join the crowd, Nature, 425, pp. 27-28, (2003)
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