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相关概念视频

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
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
The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

12.9K
The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:
12.9K

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相关实验视频

Updated: Jul 6, 2025

Mapping the Binding Site of an Aptamer on ATP Using MicroScale Thermophoresis
08:09

Mapping the Binding Site of an Aptamer on ATP Using MicroScale Thermophoresis

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AptaDB:一个全面的数据库,集成aptamer-target交互.

Long Chen1, Zhuohang Yu1, Zengrui Wu1

  • 1Shanghai Frontiers Science Center of Optogenetic Techniques for Cell Metabolism, Shanghai Key Laboratory of New Drug Design, School of Pharmacy, East China University of Science and Technology, Shanghai 200237, China.

RNA (New York, N.Y.)
|January 2, 2024
PubMed
概括
此摘要是机器生成的。

一个新的数据库,AptaDB,集成了多种aptamer数据,包括相互作用和属性. 本资源支持计算型阿普塔默设计和查,促进药理学和医学的进步.

关键词:
标注注释 标注注释吸血体目标的相互作用.我们的数据库数据库数据库数据库.类似的体.

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Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins
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相关实验视频

Last Updated: Jul 6, 2025

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In Vitro Selection of Aptamers to Differentiate Infectious from Non-Infectious Viruses
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科学领域:

  • 生物技术是生物技术.
  • 生物信息学是一种生物信息学.
  • 计算生物学 计算生物学

背景情况:

  • 亚胺在药理学,医学和分析化学方面表现出巨大的潜力.
  • 缺少集成数据阻碍了计算应用器的开发和重复使用.
  • 现有的aptamer数据库缺乏全面的,验证的信息.

研究的目的:

  • 开发一个全面的,公开访问的aptamer相关数据数据库.
  • 为了促进计算方法和aptamer重复使用.
  • 为体研究提供一个用户友好的资源.

主要方法:

  • 从文献中手动收集和整合经过实验验证的数据.
  • 包括六个关键的数据组件:阿普坦 - 目标相互作用,特性,结构,目标,实验活动和类似的阿普坦.
  • 开发了一个用户友好的数据访问界面.

主要成果:

  • AptaDB 包含 1350 个阿巴 - 目标相互作用, 1230 个结合亲和常数和 1293 个阿巴序列.
  • 与现有的aptamer数据库相比,该数据库的条目数量是现有的两倍.
  • 独特的集成不同类型的aptamer数据类别.

结论:

  • AptaDB提供了一个独特而全面的资源,用于aptamer研究.
  • 该数据库预计将成为合理的aptamer设计和选的强大工具.
  • AptaDB将不断更新,以反映aptamer研究的进步.