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相关概念视频

Amyloid Fibrils03:03

Amyloid Fibrils

9.6K
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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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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Protein Complex Assembly02:41

Protein Complex Assembly

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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
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Protein and Protein Structure02:15

Protein and Protein Structure

79.8K
Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
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Protein Organization01:13

Protein Organization

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Overview
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Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain
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粉样蛋白和蛋白质聚合物

Sara Linse1, Tuomas Knowles2

  • 1Lund University, Biochemistry & Structural Biology Chemical Centre Lund Sweden sara.linse@biochemistry.lu.se.

Chemical science
|June 23, 2023
PubMed
概括
此摘要是机器生成的。

许多不相关的蛋白质可以形成粉样纤维,这是神经退行性疾病的标志. 最近的机械学发现开始揭开粉样蛋白形成的复杂过程.

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科学领域:

  • 蛋白质科学是一种蛋白质科学.
  • 分子生物学分子生物学
  • 神经退行性疾病研究

背景情况:

  • 蛋白质科学中的一个重要发现是各种蛋白质和的倾向在体内和体外形成粉样纤维的倾向.
  • 粉样纤维素被认为是流行神经退行性疾病 (如阿尔茨海默氏症和帕金森症) 的病理标志.

研究的目的:

  • 突出最近的关键机制发现,揭开了粉样蛋白形成过程的神秘性.
  • 提供了解氨基基基因的当前进展的概述.

主要方法:

  • 这个主题系列综合了最近的实验和理论发现.
  • 方法可能包括结构生物学,生物物理学和基于细胞的测试来研究蛋白质聚合.

主要成果:

  • 不相关的蛋白质具有形成粉样结构的共同倾向.
  • 已经阐明了有关粉样蛋白形成的途径和因素的关键机制见解.

结论:

  • 了解粉样蛋白形成的机制对于开发针对神经退行性疾病的治疗策略至关重要.
  • 对蛋白质自我组装和纤维细胞形成的持续研究为未来的突破提供了希望.