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関連する概念動画

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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Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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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...
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Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

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Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
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Bacterial Protein Maturation01:26

Bacterial Protein Maturation

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Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
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Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

5.9K
A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
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Proteins: From Genes to Degradation02:11

Proteins: From Genes to Degradation

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Within a biological system, the DNA encodes the RNA, and the nucleotide sequence in the RNA further defines the amino acid sequence in the protein. This is referred to as “The Central Dogma of Molecular Biology” - a term coined by Francis Crick.  Central dogma is a firm principle in biology that defines the flow of genetic information within any life form. The two fundamental steps in central dogma are - transcription and translation.
Transcription is the synthesis of RNA...
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Updated: Sep 8, 2025

Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase
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Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase

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非ネイティブの構造的中間体を通してコトランスレーションタンパク質の折りたたみ

Siyu Wang1, Amir Bitran2, Ekaterina Samatova1

  • 1Department of Physical Biochemistry, Max Planck Institute for Multidisciplinary Sciences, Göttingen 37077, Germany.

Science advances
|September 5, 2025
PubMed
まとめ
この要約は機械生成です。

この研究では タンパク質が作られるときに 折り畳まれる様子を明らかにし その過程を導く 重要な相互作用を特定しました このコトランスレーション的折り畳みを理解することは,タンパク質の誤折り畳みを予測し,新しいタンパク質を設計するために不可欠です.

さらに関連する動画

Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability
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Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability

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4D Imaging of Protein Aggregation in Live Cells
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関連する実験動画

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Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase
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Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase

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Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability
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Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability

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4D Imaging of Protein Aggregation in Live Cells
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4D Imaging of Protein Aggregation in Live Cells

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科学分野:

  • 分子生物学
  • バイオ物理学
  • コンピュータ生物学

背景:

  • タンパク質の折り畳みは細胞機能に不可欠ですが,リボソーム内の翻訳 (コトランスレーション折り畳み) 時に発生します.
  • 誤った折りたたみ,病気に関連して,コトランスレーション折りたたみ経路の障害から生じる.
  • 原子レベルでこれらの経路を予測することは 重要な課題です

研究 の 目的:

  • コトランスレーションの折り畳み経路の原子的詳細を計算的に予測し,実験的に検証する.
  • 初期折りたたみの中間物質の安定化における非原生水性相互作用の役割を調査する.
  • リボソームの環境と分子チャペロンが コトランスレーションの折り畳みにどのように影響するかを理解する.

主な方法:

  • 折り畳み経路を予測する 原子学的分子動力学シミュレーション
  • 生物物理学的技術を用いた実験的検証
  • 新生ペプチドとリボソーム出口トンネルの相互作用の分析.

主要な成果:

  • 折り畳みのベクトル階層は計算的に予測され,実験的に検証されました.
  • 初期の折りたたみの中間物質は,一時的な非原生性水性相互作用によって安定化される.
  • これらの相互作用の破壊は,コトランスレーションの折りたたみを損なう.
  • シェーパーロントリガーファクターはペプチド動態を維持することで折り畳み経路を調節する.

結論:

  • 表面に露出する残留物は,コトランスレーションの折りたたみにおいてこれまで認識されていない重要な役割を果たします.
  • この発見は,タンパク質の折り畳み予測と設計を改善するための新しいツールを提供します.
  • この研究は タンパク質の生成を制御する基本的なメカニズムの 理解を深めるものです