関連する実験動画

Updated: Dec 1, 2025

Routine Collection of High-Resolution cryo-EM Datasets Using 200 KV Transmission Electron Microscope
09:49

Routine Collection of High-Resolution cryo-EM Datasets Using 200 KV Transmission Electron Microscope

Published on: March 16, 2022

5.7K

Cryo-EMによって明らかにされた沈着に対する反応として,本質的に乱れた鉄結合ペプチドの折りたたみ

Geula Davidov1,2, Gili Abelya1, Ran Zalk2

  • 1Department of Life Sciences, Ben-Gurion University of the Negev, Beer Sheva 8410501, Israel.

Journal of the American Chemical Society
|November 9, 2020
PubMed
まとめ

生物鉱物化タンパク質は,しばしば本質的に乱れていて,鉱物形成を制御します. この研究では,鉄酸化ナノ粒子と相互作用するM6Aタンパク質を視覚化し,鉱物との接触で乱れたタンパク質がどのように構造を得るか明らかにしています.

さらに関連する動画

Monitoring Conformational Dynamics of Single Unmodified Proteins using Plasmonic Nanotweezers09:33

Monitoring Conformational Dynamics of Single Unmodified Proteins using Plasmonic Nanotweezers

Published on: March 21, 2025

1.2K
Do's and Don'ts of Cryo-electron Microscopy: A Primer on Sample Preparation and High Quality Data Collection for Macromolecular 3D Reconstruction09:25

Do's and Don'ts of Cryo-electron Microscopy: A Primer on Sample Preparation and High Quality Data Collection for Macromolecular 3D Reconstruction

Published on: January 9, 2015

46.7K

関連する概念動画

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...
10.3K
Protein Folding01:22

Protein Folding

Overview
125.0K
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...
19.2K
Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
18.9K
Cryo-electron Microscopy01:28

Cryo-electron Microscopy

Conventional electron microscopy (EM) involves dehydration, fixation, and staining of biological samples, which distorts the native state of biological molecules and results in several artifacts. Also, the high-energy electron beam damages the sample and makes it difficult to obtain high-resolution images. These issues can be addressed using cryo-EM, which uses frozen samples and gentler electron beams. The technique was developed by Jacques Dubochet, Joachim Frank, and Richard Henderson, for...
4.0K
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...
85.1K