The Department of Microbiology and Immunology Seminar Series, Tuesday, Feb. 1, 3 p.m.
Gerald Stubbs, D.Phil.
Professor of Biological Sciences
Vanderbilt University School of Medicine
"Diversity and pleomorphism in structures of prions
and other amyloids”
Amyloids are misfolded proteins forming unbranched filamentous assemblies. They exhibit characteristic X-ray fiber diffraction patterns coming from beta-strands running approximately at right angles to the filament axis (cross-beta structure). Amyloid structure is much more complex and diverse than previously thought. We have examined amyloids formed from short peptides, the 40-residue Alzheimer’s A-beta peptide, the prion domain of the HET-s fungal prion protein, and the mammalian prion protein PrP. Our data clearly indicate significant structural differences brain-derived PrP amyloid and recombinant PrP amyloid, and support a diversity of cross-beta structures in amyloids in general.
Tuesday, Feb. 1
Room 1220 MRB III