About The Author

Ann McDermott's research group studies the mechanisms of several enzymes, principally through solid-state NMR spectroscopy. She has studied the opening of the active site flexible loop of the glycolytic enzyme, Triosephosphate isomerase, and its coupling to the appearance of product, using a range of biophysical probes. The compressed "non-bonded" interactions of the pre-reactive substrate on the active site of this enzyme, and the conformational dynamics, have been experimentally probed at high resolution. Analogous studies are underway for bacterial Cytochrome P450, where conformational flexibility impacts the range of chemistry carried out by the enzyme. These studies involve recent advances in high-resolution solid-state NMR spectra of uniformly or selectively isotopically enriched proteins wherein site-specific assignments allow for efficient structural, dynamic and mechanistic studies. She also studies the photosynthetic reaction center, and demonstrated for the first time a coherent, quantum mechanical photochemical mechanism for enhancement of NMR detection sensitivity by three orders of magnitude involving the primary players of electron transfer.

A Closer Look at RIPK1-RIPK3 Core Amyloids

Amyloids are fibrillar proteinaceous assemblies whose accumulation is a hallmark of several human diseases. Formation of amyloid fibrils occurs when protein monomers change their structure and clump together. This kind of irreversible polymerization can lead to the accumulation and propagation of toxic oligomeric seeds. Such accumulation of amyloid fibrils takes place in more than 20