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JC Price Lab - Projects

Protein Folding
ApoE

Protein structure determines function. As our bodies age, dysregulation of folding in the body leads to the buildup of misfolded proteins in amyloid plaques. These plaques are toxic and contribute to many diseases such as Alzheimer's, Parkinson's, and Amyloidosis. Despite the central role of folding in age and disease, little is actually known about how or why proteins misfold. In the Folding Group of the JC Price lab, we utilize the Iodine Protein Stability Assay (IPSA) to measure how stable proteins in the body fold. IPSA works by chemically unfolding proteins in differing amounts and labeling exposed amino acids with iodine. We then use mass spectrometry to quantify how much iodine is bound to each protein. From these iodine incorporation experiments, we use our software, CHalf, to generate folding curves and calculate "C½ values" which represent how much energy it takes to unfold a portion of the protein.

Apo E is another project of the Price Lab