Impacts of the charged residues mutation S48E/N62H on the thermostability and unfolding behavior of cold shock protein: insights from molecular dynamics simulation with Gō model

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• 作者：Ji-Guo Su ; Xiao-Ming Han ; Shu-Xin Zhao ; Yan-Xue Hou…
• 关键词：Electrostatic interactions ; Thermophilic protein ; Folding/unfolding ; Langevin dynamics simulation ; Coarse ; grained model
• 刊名：Journal of Molecular Modeling
• 出版年：2016
• 出版时间：April 2016
• 年：2016
• 卷：22
• 期：4
• 全文大小：1,472 KB
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• 作者单位：Ji-Guo Su (1)
  Xiao-Ming Han (1)
  Shu-Xin Zhao (1)
  Yan-Xue Hou (1)
  Xing-Yuan Li (1)
  Li-Sheng Qi (2)
  Ji-Hua Wang (2)
  
  1. College of Science, Yanshan University, Qinhuangdao, 066004, China
  2. Shandong Provincial Key Laboratory of Functional Macromolecular Biophysics, Institute of Biophysics, Dezhou University, Dezhou, 253023, China
  
• 刊物类别：Chemistry and Materials Science
• 刊物主题：Chemistry
  Computer Applications in Chemistry
  Biomedicine
  Molecular Medicine
  Health Informatics and Administration
  Life Sciences
  Computer Application in Life Sciences
  
• 出版者：Springer Berlin / Heidelberg
• ISSN：0948-5023

文摘

The cold shock protein from the hyperthermophile Thermotoga maritima (Tm-Csp) exhibits significantly higher thermostability than its homologue from the thermophile Bacillus caldolyticus (Bc-Csp). Experimental studies have shown that the electrostatic interactions unique to Tm-Csp are responsible for improving its thermostability. In the present work, the favorable charged residues in Tm-Csp were grafted into Bc-Csp by a double point mutation of S48E/N62H, and the impacts of the mutation on the thermostability and unfolding/folding behavior of Bc-Csp were then investigated by using a modified Gō model, in which the electrostatic interactions between charged residues were considered in the model. Our simulation results show that this Tm-Csp-like charged residue mutation can effectively improve the thermostability of Bc-Csp without changing its two-state folding mechanism. Besides that, we also studied the unfolding kinetics and unfolding/folding pathway of the wild-type Bc-Csp and its mutant. It is found that this charged residue mutation obviously enhanced the stability of the C-terminal region of Bc-Csp, which decreases the unfolding rate and changes the unfolding/folding pathway of the protein. Our studies indicate that the thermostability, unfolding kinetics and unfolding/folding pathway of Bc-Csp can be artificially changed by introducing Tm-Csp-like favorable electrostatic interactions into Bc-Csp.