関連する実験動画

Updated: Aug 9, 2026

Assembly of Gold Nanorods into Chiral Plasmonic Metamolecules Using DNA Origami Templates
09:17

Assembly of Gold Nanorods into Chiral Plasmonic Metamolecules Using DNA Origami Templates

Published on: March 5, 2019

金ナノ粒子の上に固定されたde novo設計のポリペプチドの集積誘発折り畳み

Daniel Aili1, Karin Enander, Johan Rydberg

  • 1Department of Physics, Chemistry and Biology, IFM, Linköping University, SE-581 83 Linköping, Sweden.

Journal of the American Chemical Society
|February 16, 2006
PubMed
まとめ

研究者は,金ナノ粒子と合成ポリペプチドを使用して新しいハイブリッド材料を開発しました. この材料は,ナノ粒子集積の切り替え可能な制御を可能にし,バイオミメティックおよびバイオセンサアプリケーションのペプチド折り畳みを誘発します.

さらに関連する動画

Direct Synthesis of EM-Visible Gold Nanoparticles in Cells for Protein Localization Analysis with Well-Preserved Ultrastructure09:22

Direct Synthesis of EM-Visible Gold Nanoparticles in Cells for Protein Localization Analysis with Well-Preserved Ultrastructure

Published on: April 28, 2023

Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids08:53

Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids

Published on: March 21, 2025

関連する概念動画

Protein Folding01:22

Protein Folding

Overview
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 Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
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...