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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 Organization01:24

Protein Organization

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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....
7.3K
Conservation of Protein Domains02:26

Conservation of Protein Domains

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Protein and Protein Structure02:15

Protein and Protein Structure

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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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Protein and Protein Structures02:15

Protein and Protein Structures

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関連する実験動画

Updated: Sep 16, 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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Published on: July 8, 2025

370

構造的および進化的制約を統合した逆折り畳みモデルでタンパク質の進化を進める

Hongyuan Fei1, Yunjia Li2, Yijing Liu2

  • 1New Cornerstone Science Laboratory, Center for Genome Editing, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing, China.

Cell
|July 8, 2025
PubMed
まとめ

AIによるタンパク質工学の制約 (AiCE) は,タンパク質の進化の効率を向上させます. この方法では,従来の技術を上回る高適合性の変異を設計するために,逆折り畳みモデルと制約を使用します.

キーワード:
AiCE アイスベースエディター最適化進化のカップリングゲノム編集高適性変異逆折り畳みタンパク質の進化構造に基づく制約

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Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
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Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules
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Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules

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関連する実験動画

Last Updated: Sep 16, 2025

Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins
05:08

Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins

Published on: July 8, 2025

370
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

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Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules
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Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules

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科学分野:

  • バイオテクノロジー
  • コンピュータ生物学
  • タンパク質工学

背景:

  • 伝統的なタンパク質工学方法は 低成功率と高コストの課題に直面しています
  • 現在のアプローチはしばしば人間の専門知識とタスク固有のモデルに依存し,スケーラビリティを制限しています.

研究 の 目的:

  • 効率的な人工タンパク質の進化のために,タンパク質工学 (AiCE) のAI情報制約を導入する.
  • AiCEの汎用性と従来のタンパク質工学方法の優位性を実証する.

主な方法:

  • 一般的なタンパク質の逆折りモデルを用いて 配列をサンプリングする.
  • 構造的および進化的制約を統合して,高適合性の変異を特定する.
  • デアミナーゼ,核定位配列,核酵素,逆転写酵素を含む様々なタンパク質工学作業に AiCE を適用する.

主要な成果:

  • 8つの異なるタンパク質工学アプリケーションで11%から88%の成功率を達成しました.
  • 新しく開発された塩基エディター: enABE8e (5-bpウィンドウ), enSdd6-CBE (1.3倍改善されたフィデリティ) と enDdd1-DdCBE (14.3倍まで改善されたミトコンドリア活性).
  • 数十から数千の残留物に対する AiCE の有効性を実証した.

結論:

  • AiCEは汎用的でユーザフレンドリーな変異設計法です.
  • AiCEは,タンパク質工学における効率性,スケーラビリティ,および一般化性を大幅に高めます.
  • 開発されたベースエディターは,精密医療と農業における応用が有望である.