Each year millions of people worldwide are diagnosed with diseases related to disordered protein folding. Normally, protein chains fold into a defined shape in order to function properly and when this process is disrupted, diseases such as Huntington's, Alzheimer's, cystic fibrosis and some forms of diabetes occur. The regulators of protein folding are called molecular chaperones, and as the name implies they have an important, but not well understood, assistive role in the process. Many molecular chaperones are essential for a cell’s survival. Some chaperones have been directly linked to the causes of genetic disorders involving misfolded proteins but others have been shown to be involved in slowing and preventing neurological diseases like Alzheimer's. Peter Stirling’s research focuses on a protein called phosducin-like protein 3 (PhLP3), shown to be involved in facilitating protein folding as it interacts with an essential chaperone called CCT. Peter aims to understand how PhLP3 affects protein folding and what functional consequences the PhLP3-CCT interaction has. Peter’s research will help answer fundamental questions about how cells efficiently generate and maintain properly folded proteins, which will ultimately help to better understand what is happening in a cell when protein folding is disordered. His results may eventually lead to better treatment for diseases associated with protein misfolding.