相关实验视频

Updated: Jul 9, 2025

Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase
08:59

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

Published on: February 12, 2019

11.3K

细胞蛋白折叠的起源和功能意义

Martin Romei1,2, Mathilde Carpentier3, Jacques Chomilier2

  • 1Institut Systématique Evolution Biodiversité (ISYEB UMR 7205), Sorbonne Université, MNHN, CNRS, EPHE, UA, Paris, France.

Journal of molecular evolution
|December 7, 2023
PubMed
概括

细胞蛋白折叠显示出混合的进化起源,其中许多是从古生物和细菌遗传的. 类真核生物也表现出加速折叠进化,特别是与多细胞性和免疫系统等关键创新相关.

关键词:
进化 进化 进化 进化 进化 进化 进化信息基因是一种信息基因.操作基因是指操作基因.蛋白质的折叠是蛋白质的折叠.蛋白质结构 蛋白质结构

更多相关视频

Interview: Protein Folding and Studies of Neurodegenerative Diseases19:50

Interview: Protein Folding and Studies of Neurodegenerative Diseases

Published on: July 16, 2008

12.9K
Combining Wet and Dry Lab Techniques to Guide the Crystallization of Large Coiled-coil Containing Proteins11:14

Combining Wet and Dry Lab Techniques to Guide the Crystallization of Large Coiled-coil Containing Proteins

Published on: January 6, 2017

8.0K

相关概念视频

Protein Folding01:22

Protein Folding

Overview
118.2K
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...
18.0K
Protein and Protein Structure02:15

Protein and Protein Structure

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...
79.6K
Protein Organization01:13

Protein Organization

Overview
138.0K
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
10.9K
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,...
9.6K