The primary cause of cystic fibrosis is a misfolding of the cystic fibrosis transmembrane regulator (CFTR). The misfolding occurs when the protein lacks the 508th amino acid, phenylalanine. Peptide sequences from the normal and mutant (?F508) CFTR proteins are being studied as part of a larger effort to identify intramolecular interactions that are most influential in protein folding. Peptides of approximately 10 amino acids each from the relevant portion of the normal and ?F508 proteins have been subjected to molecular dynamics simulations and a selection of the resulting conformations have been optimized using density functional theory. A comparison of the intramolecular interactions in the low energy forms of each peptide and the resulting structures of the normal and ?F508 forms will be presented.

Comparison of peptide fragments in the normal and ?F508 cystic fibrosis transmembrane regulator using molecular dynamics and density functional theory

246th National Meeting (2013)

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