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相关概念视频

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
Protein-protein Interfaces02:04

Protein-protein Interfaces

12.5K
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...
12.5K
Protein Networks02:26

Protein Networks

3.9K
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,...
3.9K

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相关实验视频

Updated: Jun 18, 2025

Detection of Protein Interactions in Plant using a Gateway Compatible Bimolecular Fluorescence Complementation BiFC System
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Detection of Protein Interactions in Plant using a Gateway Compatible Bimolecular Fluorescence Complementation BiFC System

Published on: September 16, 2011

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使用双 BiFC (Bi2FC) 改善了蛋白相互作用的验证.

Prakash Sivakumar1,2, Vijayaraj Vaishnavi1, Kothuri Gayatri1

  • 1CSIR-Centre for Cellular and Molecular Biology, Uppal Road, Hyderabad, 500007 India.

Physiology and molecular biology of plants : an international journal of functional plant biology
|August 5, 2024
PubMed
概括

这项研究引入了一种改进的体内方法,用于识别蛋白质相互作用,使用基于重新折叠的双分子光补充 (BiFC) 与内置的表达控制. 改进的技术提供了更可靠的检测,积极和消极的蛋白质相互作用.

关键词:
在 BiFC BiFC 中.光蛋白质是一种光蛋白质.P2A 是一个P2A.过渡式的表达式是暂时的.翻译记者翻译记者

更多相关视频

Bimolecular Fluorescence Complementation
08:54

Bimolecular Fluorescence Complementation

Published on: April 15, 2011

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Flow Cytometric Analysis of Bimolecular Fluorescence Complementation: A High Throughput Quantitative Method to Study Protein-protein Interaction
11:11

Flow Cytometric Analysis of Bimolecular Fluorescence Complementation: A High Throughput Quantitative Method to Study Protein-protein Interaction

Published on: August 15, 2013

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相关实验视频

Last Updated: Jun 18, 2025

Detection of Protein Interactions in Plant using a Gateway Compatible Bimolecular Fluorescence Complementation BiFC System
08:21

Detection of Protein Interactions in Plant using a Gateway Compatible Bimolecular Fluorescence Complementation BiFC System

Published on: September 16, 2011

25.3K
Bimolecular Fluorescence Complementation
08:54

Bimolecular Fluorescence Complementation

Published on: April 15, 2011

27.9K
Flow Cytometric Analysis of Bimolecular Fluorescence Complementation: A High Throughput Quantitative Method to Study Protein-protein Interaction
11:11

Flow Cytometric Analysis of Bimolecular Fluorescence Complementation: A High Throughput Quantitative Method to Study Protein-protein Interaction

Published on: August 15, 2013

18.4K

科学领域:

  • 分子生物学分子生物学
  • 生物化学 生物化学
  • 细胞生物学 细胞生物学

背景情况:

  • 双分子光补充 (BiFC) 是一种关键的体内技术,用于检测蛋白质-蛋白质相互作用.
  • 现有的BiFC方法往往缺乏对蛋白质表达水平的强有力的控制,可能导致不准确的相互作用结果.
  • 之前使用酵母二杂交 (Y2H) 的研究已经确定了某些蛋白质对是非相互作用的.

研究的目的:

  • 开发和验证一个改进的BiFC方法,并集成表达控制,以便更准确地进行体内蛋白相互作用分析.
  • 为了提高检测积极和消极蛋白质相互作用结果的可靠性.
  • 重新评估先前识别的非相互作用蛋白质对.

主要方法:

  • 开发一种新的BiFC测定方法,其中包括对感兴趣的蛋白质的双式表达和光记者,通过自裂分离.
  • 验证了改进的BiFC方法,以可靠地检测蛋白相互作用.
  • 与传统酵母两杂交 (Y2H) 试验进行比较分析.

主要成果:

  • 增强的BiFC方法证明了积极蛋白相互作用的稳健识别.
  • 该试验可靠地区分相互作用和非相互作用的蛋白质对,改善了缺少相互作用的检测.
  • 以前被Y2H确定为非相互作用的蛋白质对被证实在体内使用改进的BiFC技术进行相互作用.

结论:

  • 开发的双晶 BiFC 系统通过结合基本表达控制来为体内蛋白相互作用研究提供了显著的进步.
  • 这种方法提高了BiFC分析的准确性和可靠性,减少了假阳性和假阴性.
  • 这些发现挑战了先前的相互作用数据,并强调了蛋白质相互作用研究中表达正常化的重要性.