Dr Matthew G Iadanza
- Position: Senior Research Fellow
- Areas of expertise: Cryo electron microscopy, Structural biology, Amyloid fibrils, Electron microscopy method development, Bacterial outer membrane proteins
- Email: M.Iadanza@leeds.ac.uk
- Phone: +44(0)113 343 4370
- Location: 8.104 Astbury
- Website: GitHub | Twitter | LinkedIn | Googlescholar | Researchgate | ORCID
I came to the University of Leeds in 2014 to join Sheena Radford and Neil Ranson's research groups. Previously I was completing my Ph.D in the lab of Tamir Gonen, first at the University of Washington in Seattle Washington, and later at The Howard Hughes Medical Research Institute Janelia Farm Research Campus in northern Virginia, just outside Washington D.C.
After completing my BS in biology at Beloit College (Beloit, WI), I worked as a organic chemist for several startup companies, including Aileron therapeutics (Cambridge, MA), before beginning graduate school to focus on electron microscopy.
My research focuses on using cryo electron microscopy to inform on structure and function of a variety of macromolecular complexes as well as EM software, method development, and pipeline optimization.
I have two main biological areas of interest:
Under some conditions proteins can fold into non-native conformations which assemble into fibrils, tangles, and plaques that indicated in over 50 diseases, including Parkinson's, Altzheimer's, and Type II Diabetes. How a diverse range of unrealated proteins can form fibrils with similar structural features, prionic nature, and pathology is not well understood. I am working to understand the structres of these fibrils on multiple levels; individual protein subunits, protofilaments, and fibrils by using cryoEM to determine their structures at near-atomic resolution.
Bacterial outer membrane protein folding
The outer membranes of Gram-negative bacteria are studded with beta-barrel outer membrane proteins (OMPs) that play a wide variety of roles and are critical for bacterial survival and proliferation. After OMPs are synthesized and transported to the outer membrane they must be folded properly and inserted into the membrane, a task which is accomplished by the BAM complex. I recently determined the structure of the BAM complex using cryoEM and am now working on gaining further structural and functional knowledge about BAM and the other proteins that interact with it.<h4>Research projects</h4> <p>Any research projects I'm currently working on will be listed below. Our list of all <a href="https://biologicalsciences.leeds.ac.uk/dir/research-projects">research projects</a> allows you to view and search the full list of projects in the faculty.</p>
- Ph.D Biochemistry
- BS Biology