個々のバクテリアホドプシンタンパク質の展開における隠されたダイナミクス
Hao Yu1, Matthew G W Siewny1,2, Devin T Edwards1
1JILA, National Institute of Standards and Technology and University of Colorado, Boulder, CO 80309, USA.
Science (New York, N.Y.)
|March 4, 2017
まとめ
高解像度フォーススペクトロスコーピーは,バクテリアホドプシンの機械的な展開中に,以前に隠されたタンパク質のダイナミクスを明らかにした. この研究は複雑な中間状態と再折れを明らかにし,タンパク質の折りたたみエネルギーの景観を詳細に説明します.
科学分野:
- バイオ物理学
- 構造生物学
- 生物化学
背景:
- タンパク質の折り畳みは 構造状態の間の移行を含む複雑なプロセスです
- 制限された計測解像度は,一時的に定着した状態を遮断し,タンパク質の折り畳みの過度に単純化されたモデルにつながります.
- バクテリアホドプシン (Bacteriorhodopsin) は重要な膜タンパク質で,その機械的展開はタンパク質の動態を理解するために不可欠です.
研究 の 目的:
- 高解像度の力スペクトロスコーピーを用いて個々のバクテリアホドプシン分子の展開経路を再検討する.
- タンパク質の展開中の一時的な中間状態とその動態を検出し,特徴づけます.
- 新しく検出された状態の間の均衡測定を分析することによって,折り畳み自由エネルギー風景を推論する.
主な方法:
- 1マイクロ秒の解像度で最適化されたフォーススペクトロスコーピーを使った.
- 固有の脂質二層におけるバクテリアホドプシンの機械的な展開を調査する技術.
- 暫定的に定着した中間状態の間の均衡測定を行った.
主要な成果:
- バクテリアホドプシンの展開経路を 詳細に明らかにした
- 数多くの新しい中間状態が検出され,そのうちのいくつかは数個のアミノ酸によって分離されています.
- 10マイクロ秒未満の頻繁な再折りや状態の占有を含む複雑なダイナミクスを観察した.
結論:
- この研究は,膜タンパク質の機械的な展開の鋭いイメージを提供します.
- これまでに隠されていた タンパク質の動力学への 実験的アクセスを可能にします
- 詳細なエネルギー環境は タンパク質の折り畳みの基本的メカニズムに 洞察を与えてくれます
さらに関連する動画
11:55Examining the Conformational Dynamics of Membrane Proteins in situ with Site-directed Fluorescence Labeling
Published on: May 29, 2011
15.6K
08:18Author Spotlight: Unraveling Vitamin A Transport Mechanisms — Linking Liver Receptors to Vision Health Through RBPR2 and RBP4 Interactions
Published on: October 4, 2024
1.6K
関連する概念動画
01:11Channel Rhodopsins
3.4K
Most organisms use photoreceptors to sense and respond to light. Examples of photoreceptors include bacteriorhodopsins and bacteriophytochromes in some bacteria, phytochromes in plants, and rhodopsins in the photoreceptor cells of the vertebral retina. The light-sensitive property of these receptors is because of the bound chromophores, such as bilin in the phytochromes and retinal in the rhodopsins.
Rhodopsins belong to the family of cell surface proteins called G-protein coupled receptors,...
Rhodopsins belong to the family of cell surface proteins called G-protein coupled receptors,...
3.4K
01:19Protein Dynamics in Living Cells
2.8K
Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
2.8K
01:22Protein Folding
129.4K
Overview
129.4K
01:25Protein Folding
12.0K
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...
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
12.0K
03:00Molecular Chaperones and Protein Folding
20.6K
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...
The...
20.6K
01:26Bacterial Protein Maturation
646
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...
646