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相关概念视频

Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

18.0K
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.
The...
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Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

3.6K
After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
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Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

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Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
2.6K
Bacterial Protein Maturation01:26

Bacterial Protein Maturation

36
Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
36
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

3.7K
ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
3.7K
Coat Assembly and GTPases01:33

Coat Assembly and GTPases

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Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
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相关实验视频

Updated: Jul 16, 2025

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells
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In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells

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这是一种新的功能性混合链蛋白ADGroEL-SacSm.

Alisa Mikhaylina1, Natalia Lekontseva1, Victor Marchenkov1

  • 1Institute of Protein Research, Russian Academy of Sciences, Institutskaya Str. 4, 142290 Pushchino, Russia.

Molecules (Basel, Switzerland)
|September 9, 2023
PubMed
概括

研究人员通过将一个圆形的Sm-like蛋白骨干与GroEL伴侣域融合而设计了一种新型的温稳伴侣体. 这种蛋白质工程方法成功地创造了一个稳定的,功能性的混合蛋白,具有伴侣活动.

关键词:
陪伴者是一个陪伴者.域名重新排列 域名重新排列混合蛋白质 混合蛋白质 混合蛋白质蛋白质工程工程 蛋白质工程

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科学领域:

  • 蛋白质工程是一种蛋白质工程.
  • 生物化学 生物化学
  • 结构生物学是结构生物学.

背景情况:

  • 结合天然蛋白质域是一个关键的蛋白质工程策略.
  • 圆形的同类寡合蛋白为域附着提供了稳定的支架.
  • GroEL (ADGroEL) 的顶端域需要寡合化才能发挥作用.

研究的目的:

  • 研究使用圆形同类寡合体Sm-like蛋白质作为域附加的基础.
  • 通过将一个稳定的Sm-like蛋白与GroEL角域融合,创建一个功能混合蛋白.
  • 评估设计的融合蛋白的稳定性和伴侣活性.

主要方法:

  • 蛋白质工程和混合蛋白质的设计.
  • 使用来自*Sulfolobus acidocaldarius* (SacSm) 的圆形homoheptameric Sm-like蛋白作为一个支架.
  • 使用各种物理和化学方法进行表征,包括功能测试.

主要成果:

  • 成功创建和自我组织混合SacSm-ADGroEL蛋白质.
  • 展示了逐步组装:SacSm基础形成,然后是ADGroEL折叠.
  • 融合蛋白显示出伴侣活性,结合非本地蛋白质并减少热引起的聚合,类似于全长GroEL.

结论:

  • 工程融合蛋白质作为一个高效和热稳定的伴侣.
  • 这种蛋白质工程策略对于创建和稳定新型寡合蛋白质是有效的.
  • 该研究突出了使用稳定的圆形蛋白质支架用于功能域呈现的潜力.