Can native enzyme conformation act as a template for refolding of RNase A

by Bogy, Heather K.; Jayanthi, Srinivas; Thallapuranam, Suresh K.

Protein aggregation is a very important biol. process that is obsd. in several neurol. diseases. Misfolded proteins potentially clump together and become extremely toxic to the cell. This misfolding is a cause of many degenerative diseases, such as Parkinson's disease, Alzheimer's disease, and Huntington's disease. In this study, we are hypothesizing that the presence of native folding protein might assist the misfolded proteins to gain structure similar to native state. RNase A (RNase A), an enzyme that catalyzes the hydrolysis of RNA by breaking a P-O bond, was used as a model protein. Using various in vitro biophys. expts., we examine the effect of native template on the refolding denatured and reduced RNase A. Results of this study will be described in greater detail.