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
[1]  
Amani M., Moosavi-Movahedi A.A., Floris G., Longu S., Mura A., Moosavi-Nejad S.Z., Saboury A.A., Ahmad F., Comparative study of the conformational lock, dissociative thermal inactivation and stability of euphorbia latex and lentil seedling amine oxidases, Protein J, 24, pp. 183-191, (2005)
[2]  
Atyaksheva L.F., Pilipenko O.S., Chukhrai E.S., Poltorak O.M., Similarity of and differences between the mechanisms of thermal inactivation of β-galactosidases of different origins, Russ J Phys Chem A, 82, pp. 864-869, (2008)
[3]  
Atyaksheva L.F., Tarasevich B.N., Chukhrai E.S., Poltorak O.M., Thermal inactivation of alkali phosphatases under various conditions, Russ J Phys Chem A, 83, pp. 318-323, (2009)
[4]  
Barford D., Johnson L.N., The allosteric transition of glycogen phosphorylase, Nature, 340, pp. 609-616, (1989)
[5]  
Borzova V.A., Markossian K.A., Kara D.A., Kurganov B., Kinetic regime of dithiothreitol-induced aggregation of bovine serum albumin, Int J Biol Macromol, 80, pp. 130-138, (2015)
[6]  
Borzova V.A., Markossian K.A., Chebotareva N.A., Kleymenov S.Y., Poliansky N.B., Muranov K.O., Stein-Margolina V.A., Shubin V.V., Markov D.I., Kurganov B.I., Kinetics of thermal denaturation and aggregation of bovine serum albumin, PLoS ONE, 11, (2016)
[7]  
Chebotareva N.A., Effect of molecular crowding on the enzymes of glycogenolysis, Biochem (Mosc), 72, pp. 1478-1490, (2007)
[8]  
Chebotareva N.A., Harding S.E., Winzor D.J., Ultracentrifugal studies of the effect of molecular crowding by trimethylamine N-oxide on the self-association of muscle glycogen phosphorylase b, Eur J Biochem, 268, pp. 506-513, (2001)
[9]  
Chebotareva N.A., Kurganov B.I., Livanova N.B., Biochemical effects of molecular crowding, Biochem (Mosc), 69, pp. 1239-1251, (2004)
[10]  
Chebotareva N.A., Kurganov B.I., Harding S.E., Winzor D.J., Effect of osmolytes on the interaction of flavin adenine dinucleotide with muscle glycogen phosphorylase b, Biophys Chem, 113, pp. 61-66, (2005)
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