Related Experiment Video

Updated: Jul 1, 2025

Orientational Transition in a Liquid Crystal Triggered by the Thermodynamic Growth of Interfacial Wetting Sheets
06:26

Orientational Transition in a Liquid Crystal Triggered by the Thermodynamic Growth of Interfacial Wetting Sheets

Published on: May 15, 2017

7.1K

A solid beta-sheet structure is formed at the surface of FUS droplets during aging

Leonidas Emmanouilidis1,2, Ettore Bartalucci3,4, Yelena Kan5,6

  • 1Department of Biology, Institute of Biochemistry, ETH Zurich, Zurich, Switzerland. leonidas@bc.biol.ethz.ch.

Nature Chemical Biology
|March 12, 2024
PubMed
Summary

The surface of fused in sarcoma (FUS) protein droplets is critical for maturation into fibrils, a process inhibited by RNA binding and accelerated by increased surface area.

More Related Videos

Production of Membrane-Filtered Phase-Shift Decafluorobutane Nanodroplets from Preformed Microbubbles07:10

Production of Membrane-Filtered Phase-Shift Decafluorobutane Nanodroplets from Preformed Microbubbles

Published on: March 23, 2021

2.7K
Multiscale Structures Aggregated by Imprinted Nanofibers for Functional Surfaces06:14

Multiscale Structures Aggregated by Imprinted Nanofibers for Functional Surfaces

Published on: September 11, 2018

6.6K

Related Concept Videos

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,...
9.5K
Protein Folding01:22

Protein Folding

Overview
118.1K
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...
79.5K
Protein Organization01:13

Protein Organization

Overview
137.7K
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...
3.7K
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...
17.9K