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相关概念视频

Protein Folding01:25

Protein Folding

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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...
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Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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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...
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Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

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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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Bacterial Protein Maturation01:26

Bacterial Protein Maturation

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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...
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Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

5.9K
A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
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Proteins: From Genes to Degradation02:11

Proteins: From Genes to Degradation

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Within a biological system, the DNA encodes the RNA, and the nucleotide sequence in the RNA further defines the amino acid sequence in the protein. This is referred to as “The Central Dogma of Molecular Biology” - a term coined by Francis Crick.  Central dogma is a firm principle in biology that defines the flow of genetic information within any life form. The two fundamental steps in central dogma are - transcription and translation.
Transcription is the synthesis of RNA...
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相关实验视频

Updated: Sep 8, 2025

Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase
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Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase

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通过非原生结构中间体进行共转化蛋白折叠

Siyu Wang1, Amir Bitran2, Ekaterina Samatova1

  • 1Department of Physical Biochemistry, Max Planck Institute for Multidisciplinary Sciences, Göttingen 37077, Germany.

Science advances
|September 5, 2025
PubMed
概括
此摘要是机器生成的。

这项研究揭示了蛋白质如何折叠, 并确定了指导该过程的关键相互作用. 了解这种共翻译折叠对于预测蛋白质错折叠和设计新蛋白质至关重要.

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Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability
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4D Imaging of Protein Aggregation in Live Cells
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相关实验视频

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Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase
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Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase

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Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability
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Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability

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4D Imaging of Protein Aggregation in Live Cells
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4D Imaging of Protein Aggregation in Live Cells

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科学领域:

  • 分子生物学
  • 生物物理
  • 计算生物学

背景情况:

  • 蛋白质折叠对细胞功能至关重要,但是在核糖体内翻译 (共翻译折叠) 过程中发生.
  • 与疾病相关的错误折叠是由于配译折叠通路的破坏引起的.
  • 在原子层面预测这些路径仍然是一个重大挑战.

研究的目的:

  • 通过计算预测和实验验证共翻译折叠路径的原子细节.
  • 研究非原生疏水性相互作用在稳定早期折叠中间体中的作用.
  • 了解核糖体的环境和分子伴侣如何影响共翻译折叠.

主要方法:

  • 原子分子动力学模拟来预测折叠路径.
  • 使用生物物理技术进行实验验证.
  • 对新生和核糖体退出道之间的相互作用进行分析.

主要成果:

  • 折叠的向量层次是通过计算预测和实验验证的.
  • 早期的折叠中间体通过短暂的,非本源的疏水相互作用来稳定.
  • 这些相互作用的破坏会损害转化折叠.
  • 伴奏触发因子通过维持动态来调节折叠路径.

结论:

  • 表面暴露的残留物在共翻译折叠中起着至关重要的,以前未知的作用.
  • 这些发现为改善蛋白质折叠预测和蛋白质设计提供了新的工具.
  • 这项工作加深了我们对蛋白质生物生成的基本机制的理解.