Resolving the similarities and differences between the effect of structurally different actin-binding proteins on the thermodynamic properties of G-actin

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• 作者：Veronika Takács-Kollár ; Miklós Nyitrai…
• 关键词：Actin ; DSC ; Mouse twinfilin ; 1 ; Toxofilin
• 刊名：Journal of Thermal Analysis and Calorimetry
• 出版年：2017
• 出版时间：February 2017
• 年：2017
• 卷：127
• 期：2
• 页码：1261-1266
• 全文大小：
• 刊物类别：Chemistry and Materials Science
• 刊物主题：Physical Chemistry; Analytical Chemistry; Polymer Sciences; Inorganic Chemistry; Measurement Science and Instrumentation;
• 出版者：Springer Netherlands
• ISSN：1588-2926
• 卷排序：127

文摘

Differential scanning calorimetry was applied to compare the effects of mammalian twinfilin-1 or toxofilin on the thermodynamic properties of actin monomer. Although twinfilin and toxofilin have different structure and actin-binding sites, they similarly increased the thermodynamic stability of monomeric actin. The mammalian twinfilin increased, while the toxofilin did not significantly change the T_1/2 value (the width at half-height of the transition peak) during the complex formation between the actin and the monomer binding proteins. In case of toxofilin, the E_A value (activation energy) significantly increased compared to twinfilin where the activation energy was nearly insensitive to the complex formation. It seems that toxofilin can achieve its main function as an actin monomer sequestering protein by more effectively and consistently modifying the basic thermodynamic properties of the monomeric actin.