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相关概念视频

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
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

2.5K
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...
2.5K
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

5.7K
Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
5.7K
Assembly of Complex Microtubule Structures01:32

Assembly of Complex Microtubule Structures

1.8K
Complex microtubule structures are present in resting cells and in dividing cells. In resting cells, they are responsible for maintaining the cellular architecture, tracks for intracellular transport, positioning of organelles, assembly of cilia and flagella. They mediate the bipolar spindle assembly for chromosomal segregation and positioning of the cell division plate in dividing cells. The formation of microtubule complex structures depends on the cell type, cell stage, and cell function.
1.8K
Assembly of Cytoskeletal Filaments01:18

Assembly of Cytoskeletal Filaments

19.4K
Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
19.4K
Mechanism of Lamellipodia Formation01:31

Mechanism of Lamellipodia Formation

2.5K
Cells migrating in response to external stimuli form lamellipodia, which are thin membrane protrusions supported by a mesh of linked, branched, or unbranched actin filaments. These actin filaments interact with myosin motor proteins, creating the dynamic actomyosin complex within the cytoskeleton. Contractility, or the ability to generate contractile stress, is inherent to the actomyosin complex. It helps cells detect the stiffness of the surrounding ECM and exert contractile force for...
2.5K

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相关实验视频

Updated: Jun 24, 2025

Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry
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Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry

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复杂的路径驱动多能Fmoc-Leucine自组件.

Subir Paul1, Kousik Gayen1, Pau Gil Cantavella1

  • 1Institute of Advanced Materials, Universitat Jaume I, Avinguda de Vicent Sos Baynat, s/n, 12006, Castelló de la Plana, Castelló, Spain.

Angewandte Chemie (International ed. in English)
|June 3, 2024
PubMed
概括
此摘要是机器生成的。

科学家们控制分子自我组装路径,以创建多样化的非平衡材料. 这种方法允许相同的单体形成短暂的水凝,稳定的水凝或晶体结构,提供新的仿生材料设计可能性.

关键词:
非传统的核化.路径的复杂性 路径的复杂性没有平衡的不平衡.软材料是一种柔软的材料.这是一个超分子的超分子.

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Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
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Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

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In Situ Detection of Ribonucleoprotein Complex Assembly in the C. elegans Germline using Proximity Ligation Assay
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In Situ Detection of Ribonucleoprotein Complex Assembly in the C. elegans Germline using Proximity Ligation Assay

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相关实验视频

Last Updated: Jun 24, 2025

Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry
05:58

Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry

Published on: July 17, 2019

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Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
07:26

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

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In Situ Detection of Ribonucleoprotein Complex Assembly in the C. elegans Germline using Proximity Ligation Assay
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In Situ Detection of Ribonucleoprotein Complex Assembly in the C. elegans Germline using Proximity Ligation Assay

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科学领域:

  • 材料科学 材料科学 材料科学
  • 超分子化学 超分子化学
  • 生物模拟系统 生物模拟系统

背景情况:

  • 大自然通过复杂的途径实现了多样化的功能性非平衡自我组装.
  • 对路径复杂性的合成控制以避免热力学平衡仍然是一个挑战.

研究的目的:

  • 通过使用替代途径,从相同的单体中演示多功能非平衡组合.
  • 为了实现自组装结果的按需控制,与平衡结构分离.

主要方法:

  • 使用经典和非经典的核化路径来启动组装.
  • 使用初始的化学和热输入来引导单体沿着特定的路径.
  • 通过化学或热刺激调整动态,以控制溶解或动力捕获.

主要成果:

  • 从相同的单体中成功生成了不同的元稳定 (过渡性水凝),动力 (稳定水凝) 和热力学 (晶体,2D板) 结构.
  • 证明了初始条件决定了组装路径,导致非平衡分子排列.
  • 展示了动态捕获水凝或直接组装到平衡产品的能力.

结论:

  • 开发了一种多用途的方法来控制自组装路径,以产生各种非平衡软材料.
  • 这种方法为仿生系统提供了创造具有可调节性质的新材料的潜力.
  • 这些发现为设计具有特定过渡性或稳定性特征的材料打开了道路.