  The folding of the cholesterol trapping apolipoprotein A1 in aqueous solution
at increasing ionic strength is studied using atomically detailed molecular
dynamics simulations. We calculate various structural properties to
characterize the conformation of the protein, such as the radius of gyration,
the radial distribution function and the end to end distance. Additionally we
report information using tools specifically tailored for the characterization
of proteins, such as the mean smallest distance matrix and the Ramachandran
plot. We find that two qualitatively different configurations of this protein
are preferred, one where the protein is extended, and one where it forms loops
or closed structures. It is argued that the latter promote the association of
the protein with cholesterol and other fatty acids.
