title: Optimal local propensities for model proteins.
abstract: Lattice models of proteins were used to examine the role of local propensities in stabilizing the native state of a protein, using techniques drawn from spin-glass theory to characterize the free-energy landscapes. In the strong evolutionary limit, optimal conditions for folding are achieved when the contributions from local interactions to the stability of the native state is small. Further increasing the local interactions rapidly decreases the foldability.
mesh_terms: D008956:Models, Chemical; D010455:Peptides / Q000737:chemistry; D017510:Protein Folding; D013816:Thermodynamics
chemical_list: D010455:Peptides