Thermostability of the N-Terminal RNA-Binding Domain of the SARS-CoV Nucleocapsid Protein: Experiments and Numerical Simulations

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Title:	Thermostability of the N-Terminal RNA-Binding Domain of the SARS-CoV Nucleocapsid Protein: Experiments and Numerical Simulations
Authors:	Fang,HJ;Chen,YZ;Li,MS;Wu,MC;Chang,CL;Chang,CK;Hsu,YI;Huang,TH;Chen,HM;Tsong,TY;Hu,CK
Contributors:	數據分析方法研究中心
Keywords:	ACUTE RESPIRATORY SYNDROME;CHEMICAL-SHIFTS;FORCE QUENCH;FINITE-SIZE;CORONAVIRUS;SEQUENCE;VIRUS;COOPERATIVITY;MECHANISM;PATHWAYS
Date:	2009
Issue Date:	2010-06-29 19:12:38 (UTC+8)
Publisher:	中央大學
Abstract:	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.
Relation:	BIOPHYSICAL JOURNAL
Appears in Collections:	[Research Center for adaptive Data analysis ] journal & Dissertation

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