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相关概念视频

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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相关实验视频

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

在蛋白质-蛋白质接口上,托芬加速电子流通过蛋白质-蛋白质接口.

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
概括

这项研究表明,蛋白质二极体通过界面基跳加速电子转移 (ET). 这种在金属标记的青中观察到的跳跃机制,对于蛋白质复合体中长距离电荷分离至关重要.

更多相关视频

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

相关实验视频

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

科学领域:

  • 生物化学 生物化学
  • 生物物理学的生物物理.
  • 蛋白质工程是指蛋白质工程.

背景情况:

  • 蓝铜蛋白,如阿祖林,是重要的电子转移剂.
  • 了解蛋白质中的远程电子转移 (ET) 是生物能源学的关键.
  • 金属标记提供了一个探测蛋白质内ET通路的工具.

研究的目的:

  • 为了研究光诱导的电子转移在一个新型的金属标记青.
  • 阐明蛋白质接口和托在中介ET中的作用.
  • 为了确定最佳的氧化还原单元放置,以实现高效的电荷分离.

主要方法:

  • 一个 (Re) 复合物的特定位点共价附着在H126.6的亚苏林上.
  • 频谱分析 (UV-Vis吸收,光) 用于监测ET动力学.
  • 溶液质谱学和X射线晶体学以表征蛋白质的寡合化和结构.

主要成果:

  • 一种金属标记的亚苏林,Re126W122Cu(I),通过三个氧化还原位 (Re,W122,Cu) 创建.
  • Re染色体的光激发诱导了快速的Cu (<50 ns) 氧化.
  • 电子转移主要发生在蛋白质二极体中,由分子间托在接口上跳跃促进,加速前进ET,但减缓后退ET.

结论:

  • 蛋白质-蛋白质接口可以显著影响和优化电子传输速率.
  • 界面电子跳跃通过托残留物是长距离电荷分离的可行机制.
  • 这项工作为设计基于蛋白质的系统提供了洞察力,以实现高效的电荷转移应用.