I know this wasn't asked to me, but this is the way I understand what he said:

Originally posted by Scott Jensen
"reduce the search space"
Cut down on the number of possibilities that we'll have to look at. If they can cut out a large number of possible structures out right from the beginning, or a short time into the search (using data that they've collected so far), then that reduces the number of possible fold patterns they need to look at. They've just reduced their search space.

"establish the limits of the scoring functions we have been looking at"
How good are their scoring functions? IIRC, they are attempting to correlate the total energy of the resulting fold patterns with "correctness", as measured by root-mean-square deviation from the known (RMSD). If the energy that they are computing is lowest for the lowest RMSD structures, and the energies correlate well otherwise, then they can use the energy (as computed by their scoring functions) as a predictor of how close to the actual structure a given random candidate is. So they'll submit a few of the lowest-energy structures in something like CASP, and say that because their energy is low, they should be really close to the actual.

"make use of more complex scoring functions which may involve mini-energy minimizations"
Same thing, sort of. I guess they're looking at alternative ways of scoring proteins or something? That's what it sounds like to me anyway. Some of these alternates use the protein energy (not sure about the "mini-" part) and say that the close-to-actual ones are the ones with the minimal (mini-)energies.

Hope this makes some sense. Howard, is this actually even close? I think it is, but that doesn't actually mean anything.