Claim: Lifson–Roig model is a helix-coil transition model applied to the alpha helix-random coil transition of polypeptides, a longer, continuous, unbranched peptide, and is one of the first two in a series analogous transfer-matrix methods in polymer science that have also been applied to nucleic acids and branched polymers.
Evidence: In polymer science, the Lifson–Roig model is a helix-coil transition model applied to the alpha helix-random coil transition of polypeptides; it is a refinement of the Zimm–Bragg model that recognizes that a polypeptide alpha helix is only stabilized by a hydrogen bond only once three consecutive residues have adopted the helical conformation. A polypeptide is a longer, continuous, unbranched peptide chain of up to approximately fifty amino acids. The Zimm–Bragg and Lifson–Roig models are but the first two in a series of analogous transfer-matrix methods in polymer science that have also been applied to nucleic acids and branched polymers.