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相关概念视频

Protein Folding01:25

Protein Folding

7.5K
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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Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

5.4K
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...
11.9K
Amyloid Fibrils03:03

Amyloid Fibrils

9.0K
Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining,...
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相关实验视频

Updated: May 10, 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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通过非原生结构介质进行共转移蛋白折叠.

Siyu Wang, Amir Bitran, Ekaterina Samatova

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    概括
    此摘要是机器生成的。

    难以预测翻译过程中的蛋白质折叠. 这项研究揭示了由非本地相互作用稳定下来的层次折叠途径,为蛋白质设计和疾病研究提供了新的工具.

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    Using SecM Arrest Sequence as a Tool to Isolate Ribosome Bound Polypeptides
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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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    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

    Published on: February 12, 2019

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    Using SecM Arrest Sequence as a Tool to Isolate Ribosome Bound Polypeptides
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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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    科学领域:

    • 分子生物学分子生物学
    • 生物物理学的生物物理.
    • 计算生物学 计算生物学

    背景情况:

    • 同转移蛋白质折叠对于细胞功能至关重要.
    • 由于翻译动态的改变,错误折叠与疾病有关.
    • 预测这些折叠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蛋白折叠的矢量层次结构.
    • 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.
    • 了解伴侣触发因子如何影响共翻译折叠.

    主要方法:

    • 折叠路径的原子级计算预测.
    • 预测的折叠中间体和相互作用的实验验证.
    • 对破坏疏水性相互作用对折叠的影响分析.
    • 研究触发因子对新生动态的影响.

    主要成果:

    • 折叠的矢量层次结构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,非本土的疏水相互作用来稳定.
    • 这些相互作用的破坏会破坏中间体的稳定,并损害蛋白质折叠.
    • 伴侣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核糖体上的蛋白质折叠中起着关键作用.
    • 这些发现提供了对共同翻译折叠的基本机制的见解.
    • 开发的工具可以改善蛋白质折叠的预测,并帮助蛋白质设计.