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相关概念视频

Protein-protein Interfaces02:04

Protein-protein Interfaces

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 polypeptide...
Protein-Protein Interfaces02:04

Protein-Protein Interfaces

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 polypeptide...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

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 to...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

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 to...
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

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,...
Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
Another mechanism for membrane domain formation involves membrane proteins interacting with cytoskeletal...

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相关实验视频

Updated: Jun 5, 2026

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy
09:30

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy

Published on: August 6, 2018

复杂的分子识别接口的剖析.

Christopher A Hunter1, Maria Cristina Misuraca, Simon M Turega

  • 1Department of Chemistry, University of Sheffield, Sheffield S3 7HF, United Kingdom. c.hunter@sheffield.ac.uk

Journal of the American Chemical Society
|December 23, 2010
PubMed
概括
此摘要是机器生成的。

这项研究量化了超分子复合体中的分子内键. 结果显示,这些键是附加性的,它们的有效性取决于化学结构,而不仅仅是几何.

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Hand Controlled Manipulation of Single Molecules via a Scanning Probe Microscope with a 3D Virtual Reality Interface
11:00

Hand Controlled Manipulation of Single Molecules via a Scanning Probe Microscope with a 3D Virtual Reality Interface

Published on: October 2, 2016

相关实验视频

Last Updated: Jun 5, 2026

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy
09:30

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy

Published on: August 6, 2018

Hand Controlled Manipulation of Single Molecules via a Scanning Probe Microscope with a 3D Virtual Reality Interface
11:00

Hand Controlled Manipulation of Single Molecules via a Scanning Probe Microscope with a 3D Virtual Reality Interface

Published on: October 2, 2016

科学领域:

  • 超分子化学 超分子化学
  • 化学生物学 化学生物学
  • 物理化学 物理化学

背景情况:

  • 超分子复合体是由非共价相互作用形成的.
  • 键在分子识别和自我组装中起着至关重要的作用.
  • 了解个体相互作用的定量贡献是设计复杂分子系统的关键.

研究的目的:

  • 为了合成和描述一系列的色氨酸-氨酸-氨酸超分子复合物,具有不同数量的分子内键.
  • 量化评估单个键对这些复合物的整体稳定性和组装的贡献.
  • 在复杂的分子识别接口中研究分子结构,键和合作关系.

主要方法:

  • 合成色氨酸和氨酸连接物与外围结合组.
  • 自动紫外线/紫外线定位以表征120种不同的超分子复合体.
  • 构建化学双突变循环以量化分子内结相互作用和有效度 (EM).

主要成果:

  • 单个键的自由能量贡献是附加的,并且与超分子结构几乎没有变化.
  • 在几何上不可能的情况下,分子内部的键是不存在的;优良的互补性不能保证高亲和力.
  • 对于分子内碳酸乙- H 键 (200 mM) 的有效度比酸二- H 键 (30 mM) 高出一个数量级.

结论:

  • 这项研究表明,分子内键是附加性的,它们对组装的影响在很大程度上独立于架构.
  • 仅仅是几何互补性并不能决定高结合亲和力,并且形状灵活性对有效度的影响有限.
  • 在H-债券类型之间有效度的显著差异表明一种补偿效应,在这种情况下,更强的债券施加更严格的几何约束,影响形成效率.