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Updated: May 9, 2025

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells
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探索基于陪伴者介导分类的治疗策略

Leandro Rocha Silva1, Sheila Oliveira de Souza2, Ana Catarina Rezende Leite2

  • 1Research Group on Biological and Molecular Chemistry, Institute of Chemistry and Biotechnology, Federal University of Alagoas, Maceió, Alagoas, Brazil.

Advances in protein chemistry and structural biology
|May 5, 2025
PubMed
概括

像Hsp40,Hsp70和Hsp90这样的分子伴侣有助于分解错误折叠的蛋白质,这对细胞健康和治疗阿尔茨海默氏症等疾病至关重要. 调节这些陪伴者提供治疗潜力,但需要谨慎的平衡.

关键词:
化学的陪伴者 化学的陪伴者热冲击蛋白质是一种热冲击蛋白质.分子的伴侣是分子的伴侣.蛋白质分离的方法蛋白质的错误折叠 蛋白质的错误折叠

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Molecular Chaperones and Protein Folding03:00

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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
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