Dr. Nadia Marano
St. Lawrence University

General Chemistry, Biochemistry, Advanced Biochemistry, Research Methods in Biochemistry
Misfolding and aggregation of proteins - Proteins fold into specific shapes that are key to their function. Proteins can unfold and misfold eventually aggregating into fibers with particular characteristics called amyloid fibers. While many proteins can do this under adverse conditions, some do so in living organisms and contribute to diseases such as Alzheimer's and Parkinson's diseases.
Interactions between lipids and proteins - Unfolded or aggregated proteins can disturb the normal structure of the lipi-containing membranes that are essential to the integrity of cells and thus contribute to cell death. In addition, the lipids in membranes can accelerate the unfolding and aggregation process of proteins aggrevating the problem.
Cellular signaling, especially the role of protein-lippid interactions and lipid rafts
Fraser Mackay: Characterizing the interactions in vitro between the amyloid protein HypF-N and liposomes composed of phosphotidylcholine and phosphotidylserine
Jane Mutoru: Insolubility of T-Cell Receptors in Human Jurkat T-Cells
Tim Errington, Joel Blanchard, Wanja Nyoro: Analysis of T cell lipids
Prinetti, A., V. Chigorno, S. Prioni, N. Loberto, N. Marano, G. Tettamanti, and S. Sonnino (2001) Changes in the lipid turnover, composition and organization, as sphingolipid-enriched membrane domains, in rat cerebellar granule cells developing in vitro. Journal of Biological Chemistry, 276: 21136-21145.
Marano, N., and Mutoru, J. (presenter) (2006). - Insolubility of T-Cell Receptors in Human Jurkat T-Cells. Poster presentation at the 231st ACS National Meeting.
Nadia Marano, Walt Jennings, and Anil Waghe. ACS Advanced Chemistry. Workshop facilitator for 30 high school teachers, Austinn, TX, July 13-16, 2008.
biking, hiking, cross country skiing, dancing
