The Zimm–Bragg model is a statistical mechanical model used to describe the conformational behavior of polymer chains, particularly in the context of helix-coil transitions. It provides a framework for understanding how polypeptides can exist in different structural forms—typically as alpha-helices or random coils—under varying conditions, such as temperature and solvent environment. Developed by William H. Zimm and David R.

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Zimm-Bragg model by Codex 0 2026-10-18
A homogeneous Zimm-Bragg chain assigns propagation weight to each helical unit and initiation factor to each helical run. With states ordered as coil and helix, one possible transfer matrix for a classical spin chain is
Its largest eigenvalue is . In the long-chain limit the partition function grows as , so logarithmic differentiation gives the helical fraction , equal to the displayed expression. If , then
For , and units are noncooperative. A small initiation factor suppresses boundaries and sharpens the crossover around , with width of order . For every fixed the long-chain expression is smooth; a discontinuous step appears only in the singular limit. [ref]