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中国科学院生物物理研究所柯莎研究组揭示两种主要的人源胞浆Hsp70巯基活性差别的分子机制（图）
人源胞浆 Hsp70 巯基活性 分子机制
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2023/2/14
2022年 11月22日，《生物化学杂志》（JBC）在线发表了中科院生物物理研究所柯莎（Sarah Perrett）研究组的研究论文，题为“Exploration of the cysteine reactivity of human inducible Hsp70 and cognate Hsc70”该研究工作是柯莎研究组对Hsp70的结构与功能的关系及Hsp70的半胱氨酸巯基反应活性长期研究获...
Understanding the allosteric mechanism of the Escherichia coli Hsp70 molecular chaperone, DnaK
Hsp70 Protein aggregation Enzyme Polypeptide Protein function Nucleotides. The ATP hydrolysis
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2014/12/11
The Hsp70 family molecular chaperones prevent protein aggregation under heat shock conditions. They are highly conserved, and have a N-terminal ATPase domain, which binds and hydrolyzes ATP, and a C-t...
Components of a Protein Machine: Allosteric Domain Assembly and a Disordered C-terminus Enable the Chaperone Functions of Hsp70
Allostery DnaK Hsp70 Intrinsic disorder Molecular chaperone Protein folding
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2014/12/10
Hsp70 molecular chaperones protect proteins from aggregation, assist in their native structure formation, and regulate stress responses in the cell. A mechanistic understanding of Hsp70 function will ...