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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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Protein Families02:47

Protein Families

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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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Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

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Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
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Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

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Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
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Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

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Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules
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計算型タンパク質設計を通して,繰り返しタンパク質の宇宙を探索する.

T J Brunette1,2, Fabio Parmeggiani1,2, Po-Ssu Huang1,2

  • 1Department of Biochemistry, University of Washington, Seattle, Washington 98195, USA.

Nature
|December 18, 2015
PubMed
まとめ

科学者は新しい繰り返しタンパク質を 設計することで タンパク質構造の広大な可能性を 探求しました 自然界は 可能なタンパク質のデザインの ほんのわずかな部分しか使っていないことを証明し 生物分子工学の新たな道を開いているのです

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科学分野:

  • 構造生物学
  • 計算によるタンパク質設計
  • タンパク質の進化

背景:

  • 分子認識やシグナル伝達などの 生物学的プロセスには 重複タンパク質が不可欠です
  • 自然に発生する重複タンパク質は様々な用途のために設計されています.
  • 可能なタンパク質構造の全範囲を理解することは,タンパク質の進化における重要な問題です.

研究 の 目的:

  • シンプルなヘリックス・ループ・ヘリックス・ループモチーフを繰り返すことによって達成可能な構造的多様性を調査する.
  • 新しい繰り返しタンパク質構造を計算的に設計し,実験的に検証できるかどうかを判断する.
  • 自然に発生する例を超えて,繰り返しタンパク質の配列と構造空間を探求する.

主な方法:

  • 計算によるタンパク質設計は,新しい繰り返しタンパク質配列を生成するために使用されました.
  • 83の計算で設計されたタンパク質が合成され,実験的に特徴づけられました.
  • テクニックには,タンパク質の安定性,溶液X線散乱,結晶構造の決定が含まれていた.

主要な成果:

  • 設計の53は単体で95°Cで安定した.
  • 43の設計は,予測された構造と一致する X線散射スペクトルを示した.
  • 15のデザインの結晶構造は,RMSDが0.7から2.5 Åである計算モデルと密接に一致することを確認した.

結論:

  • 既存の重複タンパク質は,潜在的な配列と構造空間の小さなサブセットを表しています.
  • 特定の幾何学を持つ新しい繰り返しのタンパク質は,計算的に設計することができます.
  • この研究は 生物分子工学とタンパク質設計の 可能性を広げています