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Amyloid Fibrils03:03

Amyloid Fibrils

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, normally used to...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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...
Protein Complex Assembly02:41

Protein Complex Assembly

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...
Protein Folding01:25

Protein Folding

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...
Protein Folding01:22

Protein Folding

Overview
Protein Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...

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相关实验视频

Updated: Jun 14, 2026

4D Imaging of Protein Aggregation in Live Cells
08:59

4D Imaging of Protein Aggregation in Live Cells

Published on: April 5, 2013

在拥挤的环境中蛋白质聚合.

Duncan A White1, Alexander K Buell, Tuomas P J Knowles

  • 1Department of Chemistry, University of Cambridge, Cambridge, UK.

Journal of the American Chemical Society
|March 26, 2010
PubMed
概括
此摘要是机器生成的。

生物分子的物理化学特性影响蛋白质聚合,这是阿尔茨海默氏症等疾病的关键因素. 这项研究量化了粉样纤维的生长动力学,揭示了蛋白质结构,环境和聚合倾向之间的联系.

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Monitoring Protein Aggregation Kinetics In Vivo using Automated Inclusion Counting in Caenorhabditis elegans
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Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast
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Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast

Published on: June 23, 2018

相关实验视频

Last Updated: Jun 14, 2026

4D Imaging of Protein Aggregation in Live Cells
08:59

4D Imaging of Protein Aggregation in Live Cells

Published on: April 5, 2013

Monitoring Protein Aggregation Kinetics In Vivo using Automated Inclusion Counting in Caenorhabditis elegans
06:49

Monitoring Protein Aggregation Kinetics In Vivo using Automated Inclusion Counting in Caenorhabditis elegans

Published on: December 17, 2021

Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast
11:04

Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast

Published on: June 23, 2018

科学领域:

  • 生物化学 生物化学
  • 生物物理学的生物物理.
  • 分子生物学分子生物学

背景情况:

  • 生物分子的物理化学参数对于生物过程至关重要.
  • 蛋白质自我结合成粉样纤维素与阿尔茨海默氏症和II型糖尿病等疾病有关.

研究的目的:

  • 在各种拥挤的环境中量化测量粉样纤维细胞生长的动力学.
  • 建立蛋白质聚合倾向及其结构/环境参数之间的一般关系.

主要方法:

  • 定量石英晶体微平衡测量.
  • 粉样纤维细胞生长的动态分析.
  • 理论预测和建模.理论预测和建模.

主要成果:

  • 证明了将蛋白质聚合倾向与基本结构和环境参数联系起来的一般关系.
  • 在不同的拥挤条件下量化了粉样纤维细胞生长的动力学.

结论:

  • 蛋白质聚合从根本上与分子结构和局部环境有关.
  • 了解这些关系可以提供有关疾病机制和潜在治疗点的见解.