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相关概念视频

Ligand Binding and Linkage00:49

Ligand Binding and Linkage

4.8K
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

4.2K
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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Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

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Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
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The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

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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
Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

5.7K
Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
5.7K
Ligand Binding Sites02:40

Ligand Binding Sites

12.8K
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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Updated: Jun 22, 2025

The Importance of Correct Protein Concentration for Kinetics and Affinity Determination in Structure-function Analysis
19:16

The Importance of Correct Protein Concentration for Kinetics and Affinity Determination in Structure-function Analysis

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DDAffinity:使用蛋白质3D结构预测多点突变的结合亲和力的变化.

Guanglei Yu1,2,3, Qichang Zhao1,2, Xuehua Bi1,2,3

  • 1School of Computer Science and Engineering, Central South University, Changsha 410083, China.

Bioinformatics (Oxford, England)
|June 28, 2024
PubMed
概括
此摘要是机器生成的。

一个新的神经网络DDAffinity通过分析3D结构并考虑本地和全球影响,准确地预测多个突变如何影响蛋白质结合亲和力.

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相关实验视频

Last Updated: Jun 22, 2025

The Importance of Correct Protein Concentration for Kinetics and Affinity Determination in Structure-function Analysis
19:16

The Importance of Correct Protein Concentration for Kinetics and Affinity Determination in Structure-function Analysis

Published on: March 17, 2010

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Fluorescence Anisotropy as a Tool to Study Protein-protein Interactions
10:44

Fluorescence Anisotropy as a Tool to Study Protein-protein Interactions

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Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
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科学领域:

  • 计算生物学 计算生物学
  • 结构生物信息学 结构生物信息学
  • 机器学习 机器学习

背景情况:

  • 突变通过改变蛋白质的稳定性,相互作用,结构,功能和表达来推动进化.
  • 现有的计算方法由于复杂的协同作用的表现而难以预测多点突变的影响.

研究的目的:

  • 开发一种新的计算方法,DDAffinity,用于预测由多点突变引起的蛋白质结合亲和力的变化.
  • 解决现有方法的局限性,系统地考虑地方和全球的协同作用.

主要方法:

  • 开发了DDAffinity,一种通过蛋白质3D结构的神经网络传递空间和序列信息.
  • 采用k-最近邻居残留图来提取蛋白质口袋特征.
  • 采用了两步添加高斯噪声策略来捕捉全球拓特征.

主要成果:

  • 与最先进的方法相比,DDAffinity显著提高了对多点突变的预测准确性.
  • 废弃性研究证实了DDAffinity的成分的有效性.
  • 在盲测试,SARS-CoV-2变种分析和抗体优化中表现出有效性.

结论:

  • DDAffinity提供了一种强大而准确的方法来预测多个突变对蛋白质结合亲和力的影响.
  • 该方法对蛋白质工程和理解病毒进化中的应用具有前景.