Molecular chaperones combat myriad stress conditions that cause protein misfolding and aggregation and thus are essential for cell survival. These molecular chaperones are critical for maintaining the health of the proteome (termed proteostasis), which is of prime importance to human health. Defects in proteostasis are linked to many crippling diseases, including Alzheimer’s disease, Parkinson’s disease, Huntington’s disease, and ALS. Our inability to treat many of these protein-folding disorders stems, in part, from our lack of knowledge about the underlying mechanisms of molecular chaperones. My research focuses on our surprising recent discovery that RNA can function as a remarkably efficient protein chaperone. We use a combination of biochemical, structural, and genetic approaches to understand how chaperone RNAs recognize their clients, prevent protein aggregation, and aid in protein folding. These findings have important implications for our understanding of many neurodegenerative diseases.