Related Experiment Video
Updated: Aug 15, 2025

Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography
Published on: September 14, 2014
Formation of Catalytic Hotspots in ATP-Templated Assemblies
Krishnendu Das1, Haridas Kar1, Rui Chen1
1Department of Chemical Sciences, University of Padova, Via Marzolo 1, 35131 Padova, Italy.
Abstract:
The self-assembly of surfactant-based structures that rely for their formation on the combination of a thermodynamically controlled and a dissipative pathway is described. Adenosine triphosphate (ATP) acts as a high-affinity template and triggers assembly formation at low surfactant concentrations. The presence of these assemblies creates the conditions for the activation of a dissipative self-assembly process by a weak-affinity substrate. The substrate-induced recruitment of additional surfactants leads to the spontaneous formation of catalytic hotspots in the ATP-stabilized assemblies that cleave the substrate. As a result of the two self-assembly processes, catalysis can be observed at a surfactant concentration at which low catalytic activity is observed in the absence of ATP.
Related Concept Videos
ATP Synthase: Mechanism
ATP Synthase: Structure
Allosteric Proteins-ATCase
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
Protein Complex Assembly
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Assembly of Cytoskeletal Filaments
Microtubule Formation

