Symmetry breaking in a square-well bead-chain model yields marginally compact phases with alpha-helix and beta-sheet-like structures; adding side spheres produces a further phase with more complex assemblies.
Contact order, transition state placement and the refolding rates of single domain proteins
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Local symmetry determines the phases of linear chains: a simple model for the self-assembly of peptide
Symmetry breaking in a square-well bead-chain model yields marginally compact phases with alpha-helix and beta-sheet-like structures; adding side spheres produces a further phase with more complex assemblies.