Study Compares Structures of Huntington’s Disease Protein

Neutron-scattering research at the Department of Energy’s Oak Ridge National Laboratory (ORNL) has revealed clear structural differences in the normal and pathological forms of a protein involved in Huntington’s disease. Researchers conducted a side-by-side study of model protein systems in solution using a time-resolved, small-angle neutron-scattering technique at ORNL’s High Flux Isotope Reactor. The use of neutrons allowed the team to study the biological materials over time without degrading the samples’ structural integrity. The goal was to establish a baseline understanding of huntingtin’s structure in order to eventually determine the true structural basis of Huntington’s disease. The study’s results showed key differences in the ways mutant and normal huntingtin proteins take shape. The disease protein, for instance, initially forms aggregates of one to two peptides, whereas the normal version makes bigger aggregates, gathering seven or eight peptides together. To learn more about the study, click here.