Analyzing protein structures in their native environment
Proteins can fold in different ways depending on their environment. These different configurations change the function of the protein; misfolding is frequently associated with diseases such as Alzheimer’s and Parkinson’s. Until now, it has been difficult to fully characterize the different structures that proteins can take on in their natural environments. However, using a new technique known as sensitivity-enhanced nuclear magnetic resonance (NMR), MIT researchers have shown that they can analyze the structure that a yeast protein forms as it interacts with other proteins in a cell. Using this type of NMR, which is based on a technique known as dynamic nuclear polarization (DNP), scientists can gain much more insight into protein structure and function than is possible with current NMR technology, which requires large quantities of purified proteins, isolated from their usual environment. “Dynamic nuclear polarization has a capacity to transform our understanding of biological structures in their native contexts,” says Susan...