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相关概念视频

Protein-protein Interfaces02:04

Protein-protein Interfaces

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Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
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Amyloid Fibrils03:03

Amyloid Fibrils

9.6K
Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining,...
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Protein Complex Assembly02:41

Protein Complex Assembly

10.6K
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
10.6K
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...
18.0K
Protein Networks02:26

Protein Networks

4.0K
An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
4.0K
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

7.9K
Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
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相关实验视频

Updated: Jul 11, 2025

Measuring Transcellular Interactions through Protein Aggregation in a Heterologous Cell System
04:47

Measuring Transcellular Interactions through Protein Aggregation in a Heterologous Cell System

Published on: May 22, 2020

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通过接口介导的蛋白质聚合.

Fei Tao1, Qian Han1, Peng Yang1

  • 1Key laboratory of Applied Surface and Colloid Chemistry, Ministry of Education, school of Chemistry and Chemical Engineering, Shaanxi Normal University, Xi'an 710119, China. yangpeng@snnu.edu.cn.

Chemical communications (Cambridge, England)
|November 13, 2023
PubMed
概括
此摘要是机器生成的。

控制接口上的蛋白质聚合是理解生物功能和推进生物聚合物材料的关键. 本综述详细介绍了纳米尺度到宏观尺度生物聚合物结构的接口介导组装策略.

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Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast
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科学领域:

  • 生物聚合物科学 生物聚合物科学
  • 材料科学 材料科学 材料科学
  • 表面化学 表面化学

背景情况:

  • 接口上的蛋白质聚合在生理过程中起着关键作用,并可能导致功能障碍.
  • 了解对生物聚合物组装的界面影响对于生物功能和材料应用都至关重要.
  • 构建块和接口之间的相互作用的合理设计可以控制复杂的生物聚合物结构.

研究的目的:

  • 审查最近在接口介导组装和生物聚合物材料的特性方面的进展.
  • 突出控制生物聚合物组装在各种尺度 (纳米到宏观) 的策略.
  • 促进界面组装生物聚合物材料科学的整合和进步.

主要方法:

  • 检查固体液体接口 (SIL) 介导的生物聚合物组件,包括无机模板和相变.
  • 讨论由空气-水接口 (AWI) 诱导的生物聚合物组件,强调其在能量转换中的作用.
  • 液体-液体接口 (LLI) 介导的生物聚合物组件和相关应用的概述.

主要成果:

  • 控制生物聚合物的界面组装结构的进展,从纳米尺度到宏观尺度.
  • 展示各种接口类型 (SIL,AWI,LLI) 驱动特定的生物聚合物组装机制.
  • 通过界面生物聚合物材料的合理设计,识别先进应用的潜力.

结论:

  • 接口介导组装为开发先进的生物聚合物材料提供了强大的策略.
  • 对接口现象的进一步研究将推动生物聚合物科学和应用领域的创新.
  • 本次审查为未来在界面组装生物聚合物领域的进展提供了基础.