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5. Single-molecule and ensemble FRET reveals the conformational heterogeneity and allosteric mechanism

Single-molecule and ensemble FRET reveals the conformational heterogeneity and allosteric mechanism

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：slwbljcx

【摘 要】

：

　　Hsp70 is a conserved molecular chaperone which plays an indispensable role in regulating protein folding,oligomerization,and degradation in prokaryotic and

【作 者】

：

吴思[1]HongLiu[2]杨洁[1]YangJie[1]ZhangHong[1]PerrettSarah[1] 

【机 构】

：

Institute of Biophysics

【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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论文部分内容阅读

　　Hsp70 is a conserved molecular chaperone which plays an indispensable role in regulating protein folding,oligomerization,and degradation in prokaryotic and eukaryotic organisms.Hsp70 consists of an N-terminal nucleotide binding domain,a beta-sheet-containing substrate binding domain and an alpha-helical C-terminal lid domain.

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