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相关概念视频

Protein-protein Interfaces02:04

Protein-protein Interfaces

12.6K
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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Ligand Binding Sites02:40

Ligand Binding Sites

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Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
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Ligand Binding and Linkage00:49

Ligand Binding and Linkage

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Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
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Conserved Binding Sites01:49

Conserved Binding Sites

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Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
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Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

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Protein Networks02:26

Protein Networks

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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,...
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Updated: Jul 23, 2025

Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins
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使用LZerD网络服务器增强对联和多链蛋白质对接.

Kannan Harini1,2, Charles Christoffer3, M Michael Gromiha1,2

  • 1Department of Biotechnology, Bhupat and Jyoti Mehta School of Biosciences, Indian Institute of Technology Madras, Chennai, India.

Methods in molecular biology (Clifton, N.J.)
|July 14, 2023
PubMed
概括
此摘要是机器生成的。

本研究介绍了用于建模蛋白质-蛋白质复杂结构的LZerD网络服务器. 它为双向和多链对接提供了用户友好的工具,在没有实验数据的情况下帮助结构生物学研究.

关键词:
较低的德国.蛋白质的生物信息学蛋白质结构预测 蛋白质结构预测蛋白质与蛋白质的对接结构建模 结构建模对称的对接对接.网络服务器的Web服务器.

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科学领域:

  • 结构生物学 结构生物学
  • 计算生物学 计算生物学
  • 生物信息学是一种生物信息学.

背景情况:

  • 蛋白质 - 大分子相互作用对于细胞功能至关重要.
  • 缺少许多蛋白质复合物的实验确定结构.
  • 计算建模为结构预测提供了一个可行的替代方案.

研究的目的:

  • 为蛋白质复杂结构建模提供一个用户友好的Web服务器.
  • 提供对LZerD和多LZerD工具的访问,用于对联和多链对接.
  • 通过计算建模来促进蛋白质与蛋白质相互作用的研究.

主要方法:

  • 开发LZerD网络服务器.
  • 实施双向和多链蛋白质对接算法 (LZerD和Multi-LZerD).
  • 包括AttentiveDist用于单质结构建模和可视化工具.

主要成果:

  • 一个功能性的Web服务器,提供访问先进的蛋白质对接工具.
  • 用户友好的界面,可视化绑定姿势.
  • 通过单体建模,对联和多链对接的案例研究来证明其实用性.

结论:

  • LZerD 网络服务器是预测蛋白质复杂结构的宝贵资源.
  • 它使研究人员能够以计算方式建模复杂的结构,补充实验方法.
  • 服务器有助于阐明蛋白相互作用机制.