標題: Thermostability of the N-Terminal RNA-Binding Domain of the SARS-CoV Nucleocapsid Protein: Experiments and Numerical Simulations
作者: Fang, Huey-Jen
Chen, Yong-Zhong
Li, Mai Suan
Wu, Ming-Chya
Chang, Chun-Ling
Chang, Chung-ke
Hsu, Yen-ian
Huang, Tai-huang
Chen, Hueih-Min
Tsong, Tian-Yow
Hu, Chin-Kun
交大名義發表
National Chiao Tung University
公開日期: 4-三月-2009
摘要: Differential scanning calorimetry, circular dichroism spectroscopy, nuclear magnetic resonance spectroscopy, and numerical simulations were used to study the thermostability of the N-terminal RNA-binding domain (RBD) of the SARSCoV nucleocapsid protein. The transition temperature of the RBD in a mixing buffer, composed of glycine, sodium acetate, and sodium phosphate with 100 mM sodium chloride, at pH 6.8, determined by differential scanning calorimetry and circular dichroism, is 48.74 degrees C. Experimental results showed that the thermal-induced unfolding-folding transition of the RBD follows a two-state model with a reversibility >90%. Using a simple Go-like model and Langevin dynamics we have shown that, in agreement with our experiments, the folding of the RBD is two-state. Theoretical estimates of thermodynamic quantities are in reasonable agreement with the experiments. Folding and thermal unfolding pathways of the RBD also were experimentally and numerically studied in detail. It was shown that the strand 01 from the N-terminal folds last and unfolds first, while the remaining beta-strands fold/unfold cooperatively.
URI: http://dx.doi.org/10.1016/j.bpj.2008.10.045
http://hdl.handle.net/11536/7504
ISSN: 0006-3495
DOI: 10.1016/j.bpj.2008.10.045
期刊: BIOPHYSICAL JOURNAL
Volume: 96
Issue: 5
起始頁: 1892
結束頁: 1901
顯示於類別:期刊論文


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