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相关概念视频

Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

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Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
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Energy to Drive Translocation01:37

Energy to Drive Translocation

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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...
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Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

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Insertion of Single-pass Transmembrane Proteins in the RER01:26

Insertion of Single-pass Transmembrane Proteins in the RER

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Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
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Protein Transport into the Inner Mitochondrial Membrane01:34

Protein Transport into the Inner Mitochondrial Membrane

4.1K
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...
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Single-pass Transmembrane Proteins01:25

Single-pass Transmembrane Proteins

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Integral membrane proteins are tightly associated with the cell membrane and play a crucial role in cell communication, signaling, adhesion, and transport of the molecules. Some integral membrane proteins are present only in the membrane monolayer. For example, the enzyme fatty acid amide hydrolase is present in the cytoplasmic side of the membrane monolayer. In contrast, another type of integral membrane protein, also known as a transmembrane protein, spans across the membrane. Transmembrane...
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相关实验视频

Updated: Sep 10, 2025

Structure-Based Simulation and Sampling of Transcription Factor Protein Movements along DNA from Atomic-Scale Stepping to Coarse-Grained Diffusion
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Structure-Based Simulation and Sampling of Transcription Factor Protein Movements along DNA from Atomic-Scale Stepping to Coarse-Grained Diffusion

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通过人工智能引导的过渡路径采样捕获的STIM1跨膜螺旋体二分化.

Ferdinand Horvath1, Hendrik Jung2, Herwig Grabmayr3

  • 1Institute of Theoretical Physics, Johannes Kepler University Linz, 4040 Linz, Austria.

Proceedings of the National Academy of Sciences of the United States of America
|August 26, 2025
PubMed
概括

流体相互作用分子1 (STIM1) 蛋白质二元化是感应的关键. 人工智能引导的模拟揭示了三种不同的STIM1跨膜螺旋二元体配置,澄清了其机制.

关键词:
在STIM1中,TM-螺旋体的二分化在商店经营的入口.过渡路径采样 过渡路径采样

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Chemical Dimerization-Induced Protein Condensates on Telomeres
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Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
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Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

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相关实验视频

Last Updated: Sep 10, 2025

Structure-Based Simulation and Sampling of Transcription Factor Protein Movements along DNA from Atomic-Scale Stepping to Coarse-Grained Diffusion
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Chemical Dimerization-Induced Protein Condensates on Telomeres
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科学领域:

  • 生物物理学的生物物理.
  • 分子生物学分子生物学
  • 信号传递 信号传递

背景情况:

  • 流体相互作用分子1 (STIM1) 是一个关键的Ca2+传感器,位于内质网膜 (ER) 膜中.
  • ER Ca2+ 枯竭会触发STIM1的结构变化,从而启动信号通路.
  • 在这个过程中,STIM1的跨膜 (TM) 域的二元化是关键的早期步骤.

研究的目的:

  • 阐明控制STIM1跨膜螺旋体二元化的原子化机制.
  • 为了识别不同的STIM1二分体配置及其相关的过渡状态.
  • 通过实验性突变发生研究来验证模拟结果.

主要方法:

  • 利用人工智能引导的过渡路径采样 (aimmd) 进行广泛的分子动力学 (MD) 模拟.
  • 在模拟ER的脂质双层环境中进行全原子MD模拟.
  • 综合计算结果与体外光基的二分化倾向实验.

主要成果:

  • 确定了三种不同的,共存的STIM1 TM螺旋二元体配置,解决了之前的实验差异.
  • 主导的二次元配置具有X形接口,由SxxxG图案稳定.
  • 在实验试验中,SxxxG基因的突变发生改变了STIM1二分化倾向.
  • 标志着过渡状态组合,突出显示光线螺旋间接触的重要性.

结论:

  • 人工智能引导的MD模拟为罕见的分子事件提供了前所未有的原子细节,例如STIM1二分化.
  • STIM1 TM螺旋体二分化通过多个路径发生,受到光线相互作用的影响.
  • 这些发现为STIM1在细胞平衡中的作用提供了机械的理解.