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関連する概念動画

The Replisome03:01

The Replisome

33.0K
DNA replication is carried out by a large complex of proteins that act in a coordinated matter to achieve high-fidelity DNA replication. Together this complex is known as the DNA replication machinery or the replisome.
The synthesis of the leading and lagging strands is a highly coordinated process. To explain this, the “Trombone model” was proposed by Bruce Alberts in 1980. The DNA loop formation starts when a primer is synthesized on the parent lagging strand. The loop grows with...
33.0K
Restarting Stalled Replication Forks02:37

Restarting Stalled Replication Forks

5.8K
DNA replication is initiated at sites containing predefined DNA sequences known as origins of replication. DNA is unwound at these sites by the minichromosome maintenance (MCM) helicase and other factors such as Cdc45 and the associated GINS complex.The unwound single strands are protected by replication protein A (RPA) until DNA polymerase starts synthesizing DNA at the 5’ end of the strand in the same direction as the replication fork. To prevent the replication fork from falling apart,...
5.8K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

17.7K
The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
17.7K
Translesion DNA Polymerases02:10

Translesion DNA Polymerases

9.8K
Translesion (TLS) polymerases rescue stalled DNA polymerases at sites of damaged bases by replacing the replicative polymerase and installing a nucleotide across the damaged site. Doing so, TLS allows additional time for the cell to repair the damage before resuming regular DNA replication.
TLS polymerases are found in all three domains of life - archaea, bacteria, and eukaryotes. Of the different classes of TLS polymerases, members of the Y family are fitted with specialized structures that...
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DNA Helicases00:55

DNA Helicases

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DNA unwinding helicase enzymes are a type of motor protein. Motor proteins can translocate along filaments or polymers using energy generated from ATP hydrolysis. Helicases are involved in all the important cellular processes where DNA unwinding is required, such as DNA replication, repair, recombination, and transcription. They are present in all living organisms, but vary in their structure, function, and mechanism of action. For example, in prokaryotes, DnaB helicase binds and translocates...
21.1K
Homologous Recombination02:31

Homologous Recombination

50.2K
The basic reaction of homologous recombination (HR) involves two chromatids that contain DNA sequences sharing a significant stretch of identity. One of these sequences uses a strand from another as a template to synthesize DNA in an enzyme-catalyzed reaction. The final product is a novel amalgamation of the two substrates. To ensure an accurate recombination of sequences, HR is restricted to the S and G2 phases of the cell cycle. At these stages, the DNA has been replicated already and the...
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Updated: Jun 6, 2025

Chemical Triphosphorylation of Oligonucleotides
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Chemical Triphosphorylation of Oligonucleotides

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折りたたみ器と自己複製器の間の光媒介型相互変換

Yulong Jin1,2, Pradeep K Mandal3, Juntian Wu4

  • 1Beijing National Laboratory for Molecular Sciences, CAS Key Laboratory of Analytical Chemistry for Living Biosystems, Institute of Chemistry, Chinese Academy of Sciences, 100190 Beijing, China.

Journal of the American Chemical Society
|November 26, 2024
PubMed
まとめ
この要約は機械生成です。

この研究は,単一の分子の構成要素が 実験室で自己複製する繊維や 折りたたまれた分子 (折りたたみ) を形成する方法を示しています. 振動やpHの変化のような 外部刺激によって 構造が形成され 生命の起源の洞察が提供されます

さらに関連する動画

Internalization and Observation of Fluorescent Biomolecules in Living Microorganisms via Electroporation
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Internalization and Observation of Fluorescent Biomolecules in Living Microorganisms via Electroporation

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Folding and Characterization of a Bio-responsive Robot from DNA Origami
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Folding and Characterization of a Bio-responsive Robot from DNA Origami

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関連する実験動画

Last Updated: Jun 6, 2025

Chemical Triphosphorylation of Oligonucleotides
13:19

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Internalization and Observation of Fluorescent Biomolecules in Living Microorganisms via Electroporation
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Internalization and Observation of Fluorescent Biomolecules in Living Microorganisms via Electroporation

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Folding and Characterization of a Bio-responsive Robot from DNA Origami
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Folding and Characterization of a Bio-responsive Robot from DNA Origami

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科学分野:

  • 生命の研究の起源
  • 超分子化学
  • システム化学

背景:

  • 自己複製分子と 折りたたまれたマクロモレキュルは 生命の出現と進化にとって 極めて重要です
  • アビオティックなシステムにおけるこれらの構造の相互作用はよく理解されていません.

研究 の 目的:

  • 単一のビルディングブロックが 自己複製分子や 折り畳み物を作ることができる アビオティックなシステムを実証する.
  • これらの異なる構造の形成を制御する刺激を調査する.

主な方法:

  • ディスルファイドベースのダイナミック・コンビネトリアル・ライブラリを使用した.
  • メカノイジテーションを施し,pH条件を制御する.
  • 光でpHを操作する光酸を導入した

主要な成果:

  • 単一の構成要素は,振動と適度なpH下で選択的に自己複製するヘクサマー繊維を形成します.
  • 15サブユニットのマクロサイクルの折りたたみ物質は,一時的に形成され,より低いpHで,または振動なしに蓄積される.
  • 折りたたみ器と自己複製器の間の相互変換は,光によるpH変化を含む外部刺激によって達成された.

結論:

  • 単一の先駆体から自己複製体または折り畳み体を生成する制御可能な無生物系を実証した.
  • 光を含む外部の刺激が これらの状態間の移行を促す可能性を示した.
  • 生命の初期における複雑性と消耗性の構造の出現を理解するためのモデルシステムを提供した.