Chaperonin-enhanced Escherichia coli cell-free expression of functional CXCR4
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- 作者：Haixia Chia ; 1 ; haixiafengye@126.com" class="auth_mail" title="E-mail the corresponding author ; Xiaoqiang Wanga ; b ; 1 ; wangxq001@upc.edu.cn" class="auth_mail" title="E-mail the corresponding author ; Jiqiang Lia ; ljq325@163.com" class="auth_mail" title="E-mail the corresponding author ; Hao Rena ; renh@upc.edu.cn" class="auth_mail" title="E-mail the corresponding author ; Fang Huanga ; fhuang@upc.edu.cn" class="auth_mail" title="E-mail the corresponding author
- 关键词：Chaperonin ; G protein-coupled receptor ; Cell-free expression ; Protein folding ; Structural stability ; Biological activity
- 刊名：Journal of Biotechnology
- 出版年：2016
- 出版时间：10 August 2016
- 年：2016
- 卷：231
- 期：Complete
- 页码：193-200
- 全文大小：1179 K
文摘
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Synergies of the bacterial chaperonin GroEL-GroES and cell-free expression for the production of functionally folded CXCR4 is studied.
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GroEL-GroES greatly increases the rate and yield of CXCR4 functional folding.
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The structural stability and ligand binding affinity of CXCR4 can be improved with supplied GroEL-GroES.
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The cooperation between GroEL and GroES is required to promote efficient folding.
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New insights into membrane protein production and folding, as well as the role of molecular chaperones.