![]() | Noel LazoBiophysical Chemistry; NMR and Mass Spectrometry of ProteinsAssistant Professor and Carlson Chair in Chemistry Clark University Worcester, MA 01610 E-mail: Phone: 508-793-7602 Office: S335, Sackler Sciences Center |
B.S., University of the Philippines, 1981 Dr. Lazo held appointments at the College of Medicine of the University of Iowa, Center for Neurologic Diseases at Brigham and Women's Hospital, and the Department of Neurology at UCLA Dr. Lazo has been at Clark since 2006. He recently obtained a Junior Faculty Award (2007-2009) from the American Diabetes Association Current Research and TeachingResearch in my laboratory focuses on the biophysics of folding and aggregation of proteins. A combination of biophysical methods including NMR spectroscopy, limited proteolysis, hydrogen exchange and molecular modeling is used. Proteins of interest include the amyloid ß-protein in Alzheimer's disease, islet amyloid polypeptide associated with type 2 diabetes, prion protein in various forms of neurodegenerative disease, and skin proteins linked to epidermolysis bullosa, a disease characterized by skin blistering following little or no trauma. The long-term goal of our research is to develop drugs that inhibit the formation of the proximate pathogen. Other research interests include NMR spectroscopy of membrane proteins, methods development, and the structure and dynamics of amyloid fibrils. Selected Publications and PapersA. Journals Murray MM, Krone MG, Bernstein SL, Baumketner A, Condron MM, Lazo ND, Teplow DB, Wyttenbach T, Shea JE, and Bowers MT. Amyloid beta-protein: experiment and theory on the 21-30 fragment (2009). Phys. Chem. B 113(17), 6041-6046. Krone MG, Baumketner A, Bernstein SL, Wyttenbach T, Lazo ND, Teplow DB, Bowers MT, and Shea J-E. Effects of Familial Alzheimer's Disease Mutations on the Folding Nucleation of the Amyloid β-Protein (2008). J. Mol. Biol. 381, 221-228. Grant MA, Lazo ND, Lomakin A, Condron MM, Arai H, Yamin G, Rigby AC, and Teplow DB. Familial Alzheimer's disease mutations alter the stability of the amyloid ß-protein monomer folding nucleus (2007). Proc. Natl. Acad. 104, 16522-16527. |


