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Cystic Fibrosis (CF) is a common lethal genetic disorder caused by mutations in the cystic fibrosis transmembrane conductance regulator (CFTR) anion channel. Misfolding and degradation of CFTR are the hallmarks of the predominant mutation, F508del, located in the first nucleotide binding domain (NBD1). While the mutation is known to affect the thermal stability of NBD1 and assembly of CFTR domains, the molecular events that lead to misfolding of F508del-CFTR remain elusive. Here, we demonstratedoi:10.1101/2020.07.09.195099 fatcat:njlar4o4vjexvnfpq4cplsiuuq