Kz. Yue et Ka. Dill, SEQUENCE-STRUCTURE RELATIONSHIPS IN PROTEINS AND COPOLYMERS, Physical review. E, Statistical physics, plasmas, fluids, and related interdisciplinary topics, 48(3), 1993, pp. 2267-2278
We model proteins as copolymer chains of H (hydrophobic) and P (polar)
monomers configured as self-avoiding flights on three-dimensional sim
ple-cubic lattices. The HH interaction is favorable. The folding probl
em is to find the ''native'' conformation(s) (lowest free energy) for
an HP sequence. Using geometric proofs for self-avoiding lattice chain
s, we develop equations relating a monomer sequence to its native stru
ctures. These constraint relations can be used for two purposes: (1) t
o compute a tight lower bound on the free energy of the native state f
or HP sequences of any length, which is useful for testing conformatio
nal search strategies, and (2) to develop a search strategy. In its pr
esent implementation, the search strategy finds native states for HP l
attice chains up to 36 monomers in length, which is a speedup of 5 - 1
5 orders of magnitude over existing brute-force exhaustive-search meth
ods.