  Focusing on a small set of proteins that i) fold in a concerted, all-or-none
fashion and ii) do not contain knots or slipknots, we show that the Gauss
linking integral, the torsion and the number of sequence-distant contacts
provide information regarding the folding rate. Our results suggest that the
global topology/geometry of the proteins shifts from right-handed to
left-handed with decreasing folding rate, and that this topological change is
associated with an increase in the number of more sequence-distant contacts.
