Northwestern scientists shed new light on neurodegenerative diseases. A roster of apparently dissimilar neurodegenerative diseases are major challenges to neuropsychiatry: Huntington’s Disease, Alzheimer’s Disease, Creutzfelt-Jakob Disease and the other prior diseases (see below), cystic fibrosis. They all share one basic common pathway — they arise from the neurotoxic effects of the accumulation of misfolded proteins due to metabolic errors. Misfolded protein is insoluble because of its conformation change, and aggregates, and the aggregation takes down good protein with the bad in a snowballing effect. It turns out there are a class of “chaperone” molecules called heat shock proteins that function to prevent misfolding and detect already-misfolded proteins to prevent their further accumulation. Neurodegenerative diseases, new research suggests, represent the body’s losing race between the misfolding process and its supply of the protective heat shock proteins.Elucidating the role of these molecular chaperones suggests a possible avenue for prevention and remediation of this vexing class of gruesome and fatal diseases.