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Folding of the sars coronavirus spike glycoprotein immunological fragment (sars-s1b): thermodynamic and kinetic investigation correlating with three-dimensional structural modeling

文献类型:期刊论文

作者Yu, CY; Gui, CS; Luo, HB; Chen, LL; Zhang, L; Yu, H; Yang, S; Jiang, WH; Shen, JH; Shen, X
刊名Biochemistry
出版日期2005-02-08
卷号44期号:5页码:1453-1463
ISSN号0006-2960
DOI10.1021/bi0482396
通讯作者Shen, x()
英文摘要Spike glycoprotein of sars coronavirus (s protein) plays a pivotal role in sars coronavirus (sars_cov) infection. the immunological fragment of the s protein (ala251-his641, sars_s1b) is believed to be essential for sars_cov entering the host cell through s protein-ace-2 interaction. we have quantitatively characterized the thermally induced and guhcl-induced unfolding features of sars_s1b using circular dichroism (cd), tryptophan fluorescence, and stopped-flow spectral techniques. for the thermally induced unfolding at ph 7.4, the apparent activation energy (e-app) and transition midpoint temperature (t-m) were determined to be 16.3 +/- 0.2 kcal/rnol and 52.5 +/- 0.4 degreesc, respectively. the cd spectra are not dependent on temperature, suggesting that the secondary structure of sars_s1b has a relatively high thermal stability. guhcl strongly affected sars_s1b structure. both the cd and fluorescent spectra resulted in consistent values of the transition middle concentration of the denaturant (c-m ranging from 2.30 to 2.45 m) and the standard free energy change (deltagdegrees, ranging from 2.1 to 2.5 kcal/mol) for the sars_s1b unfolding reaction. moreover, the kinetic features of the chemical unfolding and refolding of sars_s1b were also characterized using a stopped-flow cd spectral technique. the obvious unfolding reaction rates and relaxation times were determined at various guhcl concentrations, and the c-m value was obtained, which is very close to the data that resulted from cd and fluorescent spectral determinations. secondary and three-dimensional structural predictions by homology modeling indicated that sars_s1b folded as a globular-like structure by beta-sheets and loops; two of the four tryptophans are located on the protein surface, which is in agreement with the tryptophan fluorescence result. the three-dimensional model was also used to explain the recently published experimental results of s1-ace-2 binding and immunizations.
WOS关键词ACUTE RESPIRATORY SYNDROME ; MASS-SPECTROMETRIC CHARACTERIZATION ; ANGIOTENSIN-CONVERTING ENZYME-2 ; CIRCULAR-DICHROISM ; MONOCLONAL-ANTIBODIES ; THERMAL-DENATURATION ; NUCLEOCAPSID PROTEIN ; BINDING DOMAIN ; HONG-KONG ; IDENTIFICATION
WOS研究方向Biochemistry & Molecular Biology
WOS类目Biochemistry & Molecular Biology
语种英语
WOS记录号WOS:000226802000009
出版者AMER CHEMICAL SOC
URI标识http://www.irgrid.ac.cn/handle/1471x/2377688
专题中国科学院大学
通讯作者Shen, X
作者单位1.Chinese Acad Sci, Grad Sch, Shanghai Inst Biol Sci,Shanghai Inst Materia Med, Drug Discovery & Design Ctr,State Key Lab Drug Re, Shanghai 20123, Peoples R China
2.Chinese Acad Sci, Grad Sch, Shanghai Inst Biol Sci, Shanghai Inst Plant Physiol & Ecol, Shanghai 200032, Peoples R China
3.E China Univ Sci & Technol, Sch Pharm, Shanghai 200237, Peoples R China
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GB/T 7714
Yu, CY,Gui, CS,Luo, HB,et al. Folding of the sars coronavirus spike glycoprotein immunological fragment (sars-s1b): thermodynamic and kinetic investigation correlating with three-dimensional structural modeling[J]. Biochemistry,2005,44(5):1453-1463.
APA Yu, CY.,Gui, CS.,Luo, HB.,Chen, LL.,Zhang, L.,...&Jiang, HL.(2005).Folding of the sars coronavirus spike glycoprotein immunological fragment (sars-s1b): thermodynamic and kinetic investigation correlating with three-dimensional structural modeling.Biochemistry,44(5),1453-1463.
MLA Yu, CY,et al."Folding of the sars coronavirus spike glycoprotein immunological fragment (sars-s1b): thermodynamic and kinetic investigation correlating with three-dimensional structural modeling".Biochemistry 44.5(2005):1453-1463.

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来源:中国科学院大学

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