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関連する概念動画

Energy to Drive Translocation01:37

Energy to Drive Translocation

Mitochondrial protein import is powered by two distinct energy sources: ATP hydrolysis and electrochemical potential across the inner membrane. Newly synthesized precursors are bound by cytosolic chaperones of the Hsp70 family, which guide them to the import receptors on the mitochondrial surface. Utilizing the energy of ATP hydrolysis, Hsp70 chaperones transfer these precursors to the TOM receptors on the mitochondrial outer membrane.
Generally, polypeptides are unfolded by two distinct...
Protein Transport to the Thylakoids01:22

Protein Transport to the Thylakoids

Thylakoids are membrane-bound sac-like structures within the chloroplast that serve as sites for photosynthesis. Thylakoid lumen contains many electron transport proteins and is enclosed by a thylakoid membrane rich in the light-harvesting complex. Proteins targeted to the thylakoids are transported as precursors and are sorted by the general TOC/TIC import pathway. Once the precursor reaches the stroma, stromal processing peptidases remove their transit signal and expose thylakoid signal...
Protein Transport into the Inner Mitochondrial Membrane01:34

Protein Transport into the Inner Mitochondrial Membrane

Nuclear encoded mitochondrial precursors are imported to the inner membrane in a multistep process involving two separate translocons, TIM22 and TIM23. TIM23 is a cation-selective pore that remains closed by the N terminal segment of the protein. Negative charges on the TIM23 act as a receptor for the incoming precursor, pulling the positively charged matrix-targeting sequence for peptide insertion and translocation.
Transport of mitochondrial precursors across the TIM23 channel is driven by...
Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Protein-Protein Interfaces02:04

Protein-Protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

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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関連する実験動画

Updated: May 7, 2026

PCR Mutagenesis, Cloning, Expression, Fast Protein Purification Protocols and Crystallization of the Wild Type and Mutant Forms of Tryptophan Synthase
09:31

PCR Mutagenesis, Cloning, Expression, Fast Protein Purification Protocols and Crystallization of the Wild Type and Mutant Forms of Tryptophan Synthase

Published on: September 26, 2020

トリプトファンが加速した電子の流れは,タンパク質とタンパク質のインターフェースを横断する.

Kana Takematsu1, Heather Williamson, Ana María Blanco-Rodríguez

  • 1Beckman Institute, California Institute of Technology , Pasadena, California 91125, United States.

Journal of the American Chemical Society
|September 17, 2013
PubMed
まとめ

この研究では,タンパク質ジマーが,界面トリプトファンホッピングを通じて電子伝送 (ET) を加速することを明らかにしました. このジャンプメカニズムは,金属ラベル付アズリンで観察され,タンパク質複合体の長距離電荷分離に不可欠です.

さらに関連する動画

Chemical Modification of the Tryptophan Residue in a Recombinant Ca2+-ATPase N-domain for Studying Tryptophan-ANS FRET
12:07

Chemical Modification of the Tryptophan Residue in a Recombinant Ca2+-ATPase N-domain for Studying Tryptophan-ANS FRET

Published on: October 9, 2021

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
10:03

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy

Published on: June 27, 2014

関連する実験動画

Last Updated: May 7, 2026

PCR Mutagenesis, Cloning, Expression, Fast Protein Purification Protocols and Crystallization of the Wild Type and Mutant Forms of Tryptophan Synthase
09:31

PCR Mutagenesis, Cloning, Expression, Fast Protein Purification Protocols and Crystallization of the Wild Type and Mutant Forms of Tryptophan Synthase

Published on: September 26, 2020

Chemical Modification of the Tryptophan Residue in a Recombinant Ca2+-ATPase N-domain for Studying Tryptophan-ANS FRET
12:07

Chemical Modification of the Tryptophan Residue in a Recombinant Ca2+-ATPase N-domain for Studying Tryptophan-ANS FRET

Published on: October 9, 2021

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
10:03

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy

Published on: June 27, 2014

科学分野:

  • バイオケミストリー バイオケミストリー
  • バイオフィジックス 生物物理学
  • プロテイン工学は,タンパク質の

背景:

  • アズーリンのような青銅タンパク質は,重要な電子伝送剤である.
  • タンパク質における遠距離電子伝送 (ET) を理解することは,バイオエネルギー学の鍵です.
  • メタルラベリングは,タンパク質内のET経路を調査するためのツールを提供します.

研究 の 目的:

  • アズーリンのラベルを貼った新種の金属における光誘導による電子移転を調査する.
  • ETを媒介するタンパク質インターフェースとトリプトファンの役割を明らかにする.
  • 効率的な電荷分離のための最適なリドックスユニット配置を決定する.

主な方法:

  • アズーリンのH126.6でレニウム (Re) コンプレックスとアズーリンのサイト固有の共性結合.
  • ET運動を監視するために,光譜分析 (UV-Vis吸収,光) を行う.
  • タンパク質のオリゴメリゼーションと構造を特徴付けるための溶液質量スペクトロメトリとX線結晶学.

主要な成果:

  • メタルロラベルのアズリン,Re126W122Cu(Iは,3つのリドックスサイト (Re,W122インドール,Cu) で作られました.
  • Re染色体の光刺激により,迅速なCu (<50ns) の酸化が誘発された.
  • 電子移転は主にタンパク質二重体で発生し,インターフェースで分子間トリプトファンのジャンプによって促進され,前方ETを加速するが後方ETを遅らせた.

結論:

  • タンパク質対タンパク質のインターフェースは,電子伝送率を大幅に影響し,最適化することができます.
  • トリプトファン残基を通るインターフェイスの電子ホッピングは,長距離の電荷分離のための有効なメカニズムです.
  • この研究は,効率的な電荷伝送アプリケーションのためのタンパク質ベースのシステムの設計に関する洞察を提供します.