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Protein Folding01:22

Protein Folding

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Overview
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Protein Folding01:25

Protein Folding

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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...
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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....
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Protein Organization01:13

Protein Organization

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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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Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

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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...
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A Protocol for Computer-Based Protein Structure and Function Prediction
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アルファフォールドによる高精度なタンパク質構造予測

John Jumper1, Richard Evans2, Alexander Pritzel2

  • 1DeepMind, London, UK. jumper@deepmind.com.

Nature
|July 15, 2021
PubMed
まとめ

新しい計算法であるAlphaFoldは アミノ酸の配列から タンパク質の構造を正確に予測できます この突破は,構造バイオインフォマティクスとタンパク質研究における大きなボトルネックに対応しています.

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科学分野:

  • 構造生物学
  • 計算生物学
  • バイオ情報学

背景:

  • タンパク質の構造を理解することは,タンパク質の機能を解明するために極めて重要です.
  • 実験的な構造の決定は時間がかかり,既知のタンパク質配列のカバーを制限します.
  • 大規模な構造バイオインフォマティクスには正確な計算方法が必要です.

研究 の 目的:

  • 原子の精度でタンパク質の構造を予測するための計算方法を開発する.
  • 既存のタンパク質構造予測方法の限界を克服し,特に同質構造のないタンパク質を克服する.
  • 大規模な構造バイオインフォマティクスを可能にし,タンパク質の機能の理解を加速する.

主な方法:

  • ニューラルネットワークベースのモデル"AlphaFold"の開発
  • タンパク質構造に関する物理的,生物学的な知識をディープラーニングアルゴリズムに組み込む.
  • マシン・ラーニングのアプローチで 多シーケンスのアライメントを活用する

主要な成果:

  • AlphaFoldは,既知の同質構造がなくても,原子の精度でタンパク質の構造を定期的に予測する能力を示しました.
  • タンパク質構造予測の批判的評価 (CASP14) の検証では,ほとんどの場合,実験構造と競合する精度を示した.
  • この方法は既存のタンパク質構造予測技術を大幅に上回った.

結論:

  • 開発されたAlphaFoldモデルは,計算によるタンパク質構造の予測における重要な進歩を表しています.
  • この方法は,構造的なカバーのギャップを埋め,タンパク質の機能のメカニズム的理解を容易にすることができます.
  • AlphaFoldは前例のない精度で 大規模な構造バイオインフォマティクスを可能にします