CFTR (cystic fibrosis transmembrane conductance regulator) is an ATP-gated chloride ion channel in epithelial cell membranes involved in hydration of lung epithelium. Individuals with cystic fibrosis inherit a genetic mutation characterized by the deletion of phenylalanine at the 508th amino acid residue of CFTR, corresponding to the nucleotide binding domain-1 (NBD-1) of the protein. As a result of this mutation in NBD-1, CFTR proteins unfold and aggregate, leading to degradation by cellular quality-control mechanisms during transport to the cell membrane. Thus, individuals with cystic fibrosis lack CFTR proteins on their cell surfaces, causing poor hydration of lung epithelium and thickened mucus, which leads to inflammation and infection and eventual lung failure and death. Previous studies and experiments have indicated that the F508del mutation in CFTR contributes to thermodynamic destabilization of the protein and eventually unfolding and aggregation. Self-quenching biophysical assays utilizing fluorescent dyes have indicated that CFTR, specifically NBD-1, is able to bind certain small molecules with enough affinity to improve thermodynamic stability. Thus, my work with CFTR involves experimenting and characterizing the interactions between the nucleotide binding domains and small molecules in order to correct the pathological defect in individuals with cystic fibrosis.