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関連する概念動画

Protein Dynamics in Living Cells01:19

Protein Dynamics in Living Cells

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...
Electron Transport Chain: Complex III and IV01:43

Electron Transport Chain: Complex III and IV

During the electron transport chain, electrons from NADH and FADH2 are first transferred to complexes I and II, respectively. These two complexes then transfer the electrons to ubiquinol, which carries them further to complex III. Complex III passes the electrons across the intermembrane space to Cyt c, which carries them further to complex IV. Complex IV donates electrons to oxygen and reduces it to water. As electrons pass through complexes I, III, and IV, the energy released aids the pumping...
Protein Diffusion in the Membrane01:24

Protein Diffusion in the Membrane

Proteins show rotational as well as lateral diffusion across the membrane. The lateral diffusion of proteins was confirmed through the cell fusion experiment where mouse and human cells were fused, resulting in hybrid cells. When the human and mouse cells fused, the specific membrane proteins on human and mouse cells were marked with the red and green-fluorescent markers, respectively. Initially, the red and green fluorescence was located on the respective hemisphere of the cell. As time...
Fast Reactions01:27

Fast Reactions

Fast reactions occurring in times shorter than the time needed to mix reactants pose a unique challenge for investigation. In a liquid-phase continuous-flow system, reactants A and B are swiftly pushed into the mixing chamber, where mixing occurs within 1 ms. The reaction mixture then flows through an observation tube, and one measures light absorption to determine species concentrations at various points of the tube. This method is most appropriate when relatively large volumes of reactants...
ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased ATP...

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関連する実験動画

Updated: Jun 25, 2026

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy
08:03

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy

Published on: April 13, 2022

サイトクロームcにおける超高速タンパク質震動の動態.

Chen Zang1, Jeffrey A Stevens, Justin J Link

  • 1Department of Physics, Program of Biophysics, The Ohio State University, 191 West Woodruff Avenue, Columbus, Ohio, 43210, USA.

Journal of the American Chemical Society
|February 11, 2009
PubMed
まとめ

サイトクロームc

科学分野:

  • バイオケミストリー バイオケミストリー
  • タンパク質のダイナミクス
  • スペクトル顕微鏡検査です.

背景:

  • サイトクロームcは,細胞呼吸における重要なタンパク質です.
  • レドックス状態とダイナミクスを理解することは,細胞機能の鍵です.

研究 の 目的:

  • 鉄性および鉄性サイトクロームcの独特のヘムダイナミクスとタンパク質構成の変化を調査する.
  • フェムト秒刺激後の超高速なプロセスを解明する.

主な方法:

  • 紫外線に可視波長を用いたフェムト秒光譜検査.
  • サイト・ディレクテッド・ミュータゲネシス サイトクロームc.
  • ヘム調整とタンパク質のリラックスダイナミクスの分析.

主要な成果:

  • 鉄性シトクロームcは,超高速のヘムリガンド解離 (6倍から5倍の調整) と,その後の再結合 (7 ps) を示し,タンパク質の揺れと全体的な構造の変化を誘導する (13と42 psで回復).
  • 鉄性サイトクロームcは6倍ヘム調整を維持し,局所的なサイトプロセス (内部変換,振動冷却) に限られたダイナミクスを保持し,10 psで完全な基底状態回復し,全体的なリラックスを示さない.
  • タンパク質のダイナミクスは,2つの酸化還元状態の間で大きく異なっています.

さらに関連する動画

Quantifying Cytoskeleton Dynamics Using Differential Dynamic Microscopy
06:37

Quantifying Cytoskeleton Dynamics Using Differential Dynamic Microscopy

Published on: June 15, 2022

Using In Vitro Fluorescence Resonance Energy Transfer to Study the Dynamics Of Protein Complexes at a Millisecond Time Scale
10:50

Using In Vitro Fluorescence Resonance Energy Transfer to Study the Dynamics Of Protein Complexes at a Millisecond Time Scale

Published on: March 14, 2019

関連する実験動画

Last Updated: Jun 25, 2026

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy
08:03

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy

Published on: April 13, 2022

Quantifying Cytoskeleton Dynamics Using Differential Dynamic Microscopy
06:37

Quantifying Cytoskeleton Dynamics Using Differential Dynamic Microscopy

Published on: June 15, 2022

Using In Vitro Fluorescence Resonance Energy Transfer to Study the Dynamics Of Protein Complexes at a Millisecond Time Scale
10:50

Using In Vitro Fluorescence Resonance Energy Transfer to Study the Dynamics Of Protein Complexes at a Millisecond Time Scale

Published on: March 14, 2019

結論:

  • サイトクロームcのリドックス状態は,超高速のダイナミクスとコンフォメーションリラクゼーション経路を決定する.
  • 鉄質状態のダイナミクスは,鉄質状態とは異なり,重要なヘム調整変化と大規模なタンパク質の混乱を伴う.
  • これらの発見は,シトクロームcの機能的メカニズムに関する重要な洞察を提供します.