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相关概念视频

Conserved Binding Sites01:49

Conserved Binding Sites

4.4K
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...
4.4K
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

11.4K
Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
11.4K
Protein Folding01:25

Protein Folding

8.7K
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
8.7K
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

3.8K
ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
3.8K
Protein Families02:47

Protein Families

15.8K
Protein families are groups of homologous proteins; that is, they have similarities in amino acid sequences and three-dimensional structures. Protein families usually occur because of gene duplication, where an additional copy of a gene is inserted into the genome of an organism.   Mutations that change the amino acids but still allow the protein to be properly synthesized, will lead to new protein family members.   If these new proteins contain similar amino acids in key...
15.8K
Protein and Protein Structure02:15

Protein and Protein Structure

81.5K
Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
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相关实验视频

Updated: Sep 15, 2025

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific 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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佩加索斯:从序列中预测MD衍生的蛋白质灵活性

Yann Vander Meersche1, Gabriel Duval1, Gabriel Cretin1

  • 1Université Paris Cité and Université des Antilles and Université de la Réunion, INSERM, BIGR, DSIMB, Paris, France.

Protein science : a publication of the Protein Society
|July 17, 2025
PubMed
概括

预测蛋白质的灵活性对于功能至关重要. 一个新的工具PEGASUS使用蛋白质语言模型从序列中预测模拟的蛋白质动力学,弥合了实验方法留下的差距.

关键词:
深度学习是一种深度学习.分子动力学分子动力学预测蛋白质属性的预测.蛋白质动力学 蛋白质动力学蛋白质灵活性 蛋白质的灵活性蛋白质语言模型的模型基于序列的预测.

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A Protocol for Computer-Based Protein Structure and Function Prediction
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A Protocol for Computer-Based Protein Structure and Function Prediction

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Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

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相关实验视频

Last Updated: Sep 15, 2025

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific 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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A Protocol for Computer-Based Protein Structure and Function Prediction
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Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
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Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

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科学领域:

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

背景情况:

  • 蛋白质的灵活性对于生物功能至关重要.
  • 评估蛋白质动态的实验方法昂贵且有限.
  • 分子动力学 (MD) 模拟提供了对蛋白质灵活性的详细见解,并增加了数据的可用性.

研究的目的:

  • 为MD衍生蛋白质灵活性信息开发基于序列的预测器.
  • 为了弥补蛋白质序列识别和动态信息之间的差距.

主要方法:

  • 使用了ATLAS数据库和蛋白质语言模型.
  • 开发了用于预测模拟动态的ProtEin lanGuAge模型 (PEGASUS).
  • 整合了四个序列表示,以预测残留智的骨干波动,二面角偏差和局部距离差异测试.

主要成果:

  • 佩加索从蛋白质序列中预测MD衍生的关键灵活性指标.
  • 该工具集成了多个序列表示,用于增强预测.
  • 网络服务器和独立实用程序可供用户访问.

结论:

  • 佩加索提供了一种有价值的计算工具,用于预测蛋白质动态.
  • 该方法利用了蛋白质语言模型和MD模拟的进展.
  • 促进对大量序列的蛋白质灵活性进行研究.