Small heat shock protein IbpB acts as a robust chaperone in living cells by hierarchically activating its multi-type substrate-binding residues | |
Fu XM(付新苗) ; Shi XD(石小东) ; Chang ZY(昌增益) | |
2014 | |
关键词 | molecular chaperone small heat shock protein unnatural amino acid photocrosslinking |
英文摘要 | Small heat shock proteins(sHSPs),as ubiquitous molecular chaperones,are crucial for proteinhomeostasis.It is not clear why sHSPs are able to bind a wide spectrum of non-nativesubstrate proteins and how such binding is enhanced by heat shock.Here,by utilizing agenetically incorporated photo-crosslink...; 0 |
语种 | 英语 |
内容类型 | 其他 |
源URL | [http://ir.pku.edu.cn/handle/20.500.11897/46273] |
专题 | 生命科学学院 |
推荐引用方式 GB/T 7714 | Fu XM,Shi XD,Chang ZY. Small heat shock protein IbpB acts as a robust chaperone in living cells by hierarchically activating its multi-type substrate-binding residues. 2014-01-01. |
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