People | Locations | Statistics |
---|---|---|
Naji, M. |
| |
Motta, Antonella |
| |
Aletan, Dirar |
| |
Mohamed, Tarek |
| |
Ertürk, Emre |
| |
Taccardi, Nicola |
| |
Kononenko, Denys |
| |
Petrov, R. H. | Madrid |
|
Alshaaer, Mazen | Brussels |
|
Bih, L. |
| |
Casati, R. |
| |
Muller, Hermance |
| |
Kočí, Jan | Prague |
|
Šuljagić, Marija |
| |
Kalteremidou, Kalliopi-Artemi | Brussels |
|
Azam, Siraj |
| |
Ospanova, Alyiya |
| |
Blanpain, Bart |
| |
Ali, M. A. |
| |
Popa, V. |
| |
Rančić, M. |
| |
Ollier, Nadège |
| |
Azevedo, Nuno Monteiro |
| |
Landes, Michael |
| |
Rignanese, Gian-Marco |
|
Terfort, Andreas
in Cooperation with on an Cooperation-Score of 37%
Topics
Publications (6/6 displayed)
- 2021A model study on controlling dealloying corrosion attack by lateral modification of surfactant inhibitorscitations
- 2021A model study on controlling dealloying corrosion attack by lateral modification of surfactant inhibitorscitations
- 2019Mobility of charge carriers in self-assembled monolayerscitations
- 2019Noncovalent Functionalization of Carbon Substrates with Hydrogels Improves Structural Analysis of Vitrified Proteins by Electron Cryo-Microscopy.citations
- 2017Self-Perforated Hydrogel Nanomembranes Facilitate Structural Analysis of Proteins by Electron Cryo-Microscopy.citations
- 2016Transition voltages respond to synthetic reorientation of embedded dipoles in self-assembled monolayerscitations
Places of action
Organizations | Location | People |
---|
article
Noncovalent Functionalization of Carbon Substrates with Hydrogels Improves Structural Analysis of Vitrified Proteins by Electron Cryo-Microscopy.
Abstract
In electron cryo-microscopy, structure determination of protein molecules is frequently hampered by adsorption of the particles to the support film material, typically amorphous carbon. Here, we report that pyrene derivatives with one or two polyglycerol (PG) side chains bind to the amorphous carbon films, forming a biorepulsive hydrogel layer so that the number of protein particles in the vitreous ice drastically increases. This approach could be extended by adding a hydrogel-functionalized carbon nanotube network (HyCaNet, the hydrogel again being formed from the PG-pyrene derivatives), which stabilized the protein-containing thin ice films during imaging with the electron beam. The stabilization resulted in reduced particle motion by up to 70%. These substrates were instrumental for determining the structure of a large membrane protein complex.