title: Molecular dynamics of surfactant protein C: from single molecule to heptameric aggregates.
abstract: Surfactant protein C (SP-C) is a membrane-associated protein essential for normal respiration. It has been found that the alpha-helix form of SP-C can undergo, under certain conditions, a transformation from an alpha-helix to a beta-strand conformation that closely resembles amyloid fibrils, which are possible contributors to the pathogenesis of pulmonary alveolar proteinosis. Molecular dynamics simulations using the NAMD2 package were performed for systems containing from one to seven SP-C molecules to study their behavior in water. The results of our simulations show that unfolding of the protein occurs at the amino terminal, and despite this unfolding, no transition from alpha-helix to beta-strand was observed.
authors.affiliation: Department of Chemistry, University of Puerto Rico, Mayagüez, Puerto Rico 00681.
authors.forename: Eunice
authors.initials: E
authors.lastname: Ramírez
authors.forename: Alberto
authors.initials: A
authors.lastname: Santana
authors.forename: Anthony
authors.initials: A
authors.lastname: Cruz
authors.forename: Inés
authors.initials: I
authors.lastname: Plasencia
authors.forename: Gustavo E
authors.initials: GE
authors.lastname: López
mesh_terms: D003198:Computer Simulation; D008958:Models, Molecular; D011487:Protein Conformation; D037721:Pulmonary Surfactant-Associated Protein C / Q000737:chemistry*; D011663:Pulmonary Surfactants / Q000737:chemistry*; D014867:Water / Q000737:chemistry
chemical_list: D037721:Pulmonary Surfactant-Associated Protein C; D011663:Pulmonary Surfactants; D014867:Water