Thermodynamic and kinetic observation of transmembrane segments of CXCR4 binding to GroEL

来源 :中国化学会生物物理化学专业委员会第四届全国生物物理化学会议 | 被引量 : 0次 | 上传用户：xwxseven

【摘要】

：

　　The Escherichia coli molecular chaperone GroEL is an important nano-cage for protein folding.Using peptide substrates as mimetics of non-native proteins in

【作者】

：

迟海霞;王小强;李世新;任浩;徐燕;黄方;

【机构】

：

China University of Petroleum(East China)

【出处】

：

中国化学会生物物理化学专业委员会第四届全国生物物理化学会议

【发表日期】

：

2016年期

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　　The Escherichia coli molecular chaperone GroEL is an important nano-cage for protein folding.Using peptide substrates as mimetics of non-native proteins in GroEL-assisted folding has the advantage that this approach circumvents complications through kinetic competition between substrate folding and binding.

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Thermodynamic and kinetic observation of transmembrane segments of CXCR4 binding to GroEL

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