A chemist investigates how proteins assume their shape
When proteins are first made in our cells, they often exist as floppy chains until specialized cellular machinery helps them fold into the right shapes. Only after achieving this correct structure can most proteins perform their biological functions. Many diseases, including genetic disorders like cystic fibrosis and brittle bone disease, and neurodegenerative diseases like Alzheimer’s, are linked to defects in this protein folding process. Matt Shoulders, a recently tenured associate professor in the Department of Chemistry, is trying to understand how protein folding happens in human cells and how it goes wrong, in hopes of finding ways to prevent diseases linked to protein misfolding. “In the human cell, there are tens of thousands of proteins. The vast majority of proteins must eventually attain some well-defined three-dimensional structure to carry out their functions,” Shoulders says. “Protein misfolding and protein aggregation happen a lot, even in healthy cells. My research group’s interest is in...