Back to Research

Protein Aggregation
Proteins must fold correctly to adopt the proper conformation to perform their intended biological functions. In the crowded cellular environment, formation and maintenance of the correct structure becomes difficult as proteins age or folding homeostasis is impacted by stresses including heat shock, chemical insult, or mutations or modifications producing aggregation-prone proteins. Protein misfolding and aggregation contributes to many devastating human diseases including Alzheimer's, Parkinson's, Huntington's, type II diabetes, cystic fibrosis and prion-mediated infections. A family of proteins known as molecular chaperones regulates synthesis, folding, renaturation and degradation of proteins in cells. Our lab is interested in molecular aspects of protein aggregation in aging and diseaseincluding structure and fucntion of heat shock proteins and structural information about resulting amyloid aggregates.

Current Researchers
Ezelle McDonald, Graduate Student. My research interest lies in the mechanism and structure of heat shock proteins. To study heat shock proteins, I use site-directed spin labeling in conjunction with EPR.
Recent Publications
Nathan J. Cobb, Frank D. Sönnichsen, Hassane Mchaourab, and Witold K. Surewicz. Molecular architecture of human prion protein amyloid: A parallel, in-register -structure. PNAS. November 19, 2007.
Shi J, Koteiche HA, Mchaourab HS, Stewart PL. Cryoelectron microscopy and EPR analysis of engineered symmetric and polydisperse Hsp16.5 assemblies reveals determinants of polydispersity and substrate binding. J Biol Chem. 2006 Dec 29;281(52):40420-8. Epub 2006 Oct 31. PMID: 17079234

Koteiche HA, Mchaourab HS. Mechanism of a hereditary cataract phenotype. Mutations in alphaA-crystallin activate substrate binding. J Biol Chem. 2006 May 19;281(20):14273-9. Epub 2006 Mar 12. PMID: 16531622