Related Experiment Video
Updated: Feb 10, 2026

Generation of Native, Untagged Huntingtin Exon1 Monomer and Fibrils Using a SUMO Fusion Strategy
Published on: June 27, 2018
A Liquid to Solid Phase Transition Underlying Pathological Huntingtin Exon1 Aggregation
Thomas R Peskett1, Frédérique Rau2, Jonathan O'Driscoll1
1Institute of Structural and Molecular Biology, Birkbeck College and University College London, London, WC1E 7HX, UK.
Abstract:
Huntington's disease is caused by an abnormally long polyglutamine tract in the huntingtin protein. This leads to the generation and deposition of N-terminal exon1 fragments of the protein in intracellular aggregates. We combined electron tomography and quantitative fluorescence microscopy to analyze the structural and material properties of huntingtin exon1 assemblies in mammalian cells, in yeast, and in vitro. We found that huntingtin exon1 proteins can form reversible liquid-like assemblies, a process driven by huntingtin's polyQ tract and proline-rich region. In cells and in vitro, the liquid-like assemblies converted to solid-like assemblies with a fibrillar structure. Intracellular phase transitions of polyglutamine proteins could play a role in initiating irreversible pathological aggregation.
Related Concept Videos
Phase Transitions
Phase Transitions: Sublimation and Deposition
Phase Transitions: Melting and Freezing
Phase Transitions: Vaporization and Condensation
Molecular Comparison of Gases, Liquids, and Solids
Phase Diagrams

![Solid-phase Synthesis of [4.4] Spirocyclic Oximes](/_next/image?url=https%3A%2F%2Fcloudfront.jove.com%2FCDNSource%2Fteasers%2F58508.jpg&w=3840&q=50)