Related Experiment Video
Updated: Sep 2, 2025

Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry
Published on: July 17, 2019
Clustering of self-thermophilic asymmetric dimers: the relevance of hydrodynamics
Sergi Roca-Bonet1, Martin Wagner1, Marisol Ripoll1
1Theoretical Physics of Living Matter, Institute of Biological Information Processing, Forschungszentrum Jülich, 52425 Jülich, Germany. m.ripoll@fz-juelich.de.
Abstract:
Self-thermophilic dimers are characterized by a net phoretic attraction which, in combination with hydrodynamic interactions, results in the formation of crystalline-like aggregates. To distinguish the effect of the different contributions is frequently an important challenge. We present a simulation investigation done in parallel in the presence and the absence of hydrodynamic interactions for the case of asymmetric self-thermophoretic dimers. In the absence of hydrodynamics, the clusters have the standard heads-in configurations. In contrast, in the presence of hydrodynamics, clusters with heads-in conformation are being formed, in which dimers with their propulsion velocity pointing out of the cluster are assembled and stabilized by strong hydrodynamic osmotic flows. Significant variation in the material properties is to be expected from such differences in the collective behavior, whose understanding and control is of great relevance for the development of new synthetic active materials.
More Related Videos
Related Concept Videos
Diversity of Archaea IV
Diversity of Archaea III
Hyperthermophilic Bacteria
Noncovalent Attractions in Biomolecules
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...
Protein Folding
Molecular Chaperones and Protein Folding
The...

