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関連する概念動画

Protein Networks02:26

Protein Networks

4.1K
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,...
4.1K
Conserved Binding Sites01:49

Conserved Binding Sites

4.3K
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...
4.3K
Protein Organization01:24

Protein Organization

7.0K
Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence....
7.0K
Protein-protein Interfaces02:04

Protein-protein Interfaces

13.2K
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...
13.2K
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

11.3K
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...
11.3K
Protein Families02:47

Protein Families

15.7K
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...
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Updated: Sep 10, 2025

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
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Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

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大規模なタンパク質データベースは,構造的な互補性と機能的な局所性を明らかにする.

Paweł Szczerbiak1,2, Lukasz M Szydlowski1,2, Witold Wydmański2,3

  • 1Sano Centre for Computational Medicine, Kraków, Poland.

Nature communications
|August 25, 2025
PubMed
まとめ
この要約は機械生成です。

研究者は,アルファフォールドタンパク質構造データベースとマイクロバイオーム免疫プロジェクトからタンパク質の構造をマッピングしました. 異なるが機能的に重なり合っている タンパク質の空間を発見し 共有された生物学的機能の風景を明らかにしました

さらに関連する動画

A Protocol for Computer-Based Protein Structure and Function Prediction
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関連する実験動画

Last Updated: Sep 10, 2025

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
07:08

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

7.4K
A Protocol for Computer-Based Protein Structure and Function Prediction
16:41

A Protocol for Computer-Based Protein Structure and Function Prediction

Published on: November 3, 2011

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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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科学分野:

  • 計算生物学
  • 構造バイオインフォマティクス
  • タンパク質科学

背景:

  • タンパク質構造の予測における最近の進歩は,数多くの3Dモデルを生み出しています.
  • 大量のタンパク質構造データセットを分析するには 効率的な計算方法が不可欠です
  • AlphaFold Protein Structure Database (AFDB) やMicrobiome Immunity Project (MIP) のようなデータベースは 構造に関する貴重な情報を提供しています

研究 の 目的:

  • タンパク質の構造空間を統一した低次元の表現を開発する.
  • 様々なデータベースからタンパク質クラスタの機能プロフィールを分析し,視覚化します.
  • タンパク質の配列構造と機能の関係を探求するためのアクセシブルなツールを提供すること.

主な方法:

  • AFDBとMIPの構造クラスターを利用した.
  • タンパク質の構造に 凝固した低次元埋め込みを開発した.
  • タンパク質の構造空間に機能的な注釈をマップした.
  • データ探査のためのオープンアクセスWebサーバーを作成しました.

主要な成果:

  • AFDBとMIPのタンパク質構造は異なる領域を占めるが,機能的プロフィールでは著しく重複している.
  • 高レベルの生物学的機能は タンパク質の特定の領域に局限しています
  • この研究は,様々なタンパク質のデータ源に共通する機能的な風景を明らかにしています.
  • 更に生物学的発見のためのアプローチの汎用性を示した.

結論:

  • 開発されたタンパク質構造の表現は,配列-構造-機能関係の理解を容易にする.
  • この発見は,多様なタンパク質のデータセット内の共通の機能的組織を強調しています.
  • オープンアクセスのウェブサーバーは,分類学,環境,機能に関する新しい生物学的な質問を可能にします.