  The simulation of a protein's folding process is often done via stochastic
local search, which requires a procedure to apply structural changes onto a
given conformation. Here, we introduce a constraint-based approach to enumerate
lattice protein structures according to k-local moves in arbitrary lattices.
Our declarative description is much more flexible for extensions than standard
operational formulations. It enables a generic calculation of k-local neighbors
in backbone-only and side chain models. We exemplify the procedure using a
simple hierarchical folding scheme.
