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Helix-coil transition model

Helix-coil transition models are formalized techniques in statistical mechanics developed to describe conformations of linear polymers in solution. The models are usually but not exclusively applied to polypeptides as a measure of the relative fraction of the molecule in an alpha helix conformation versus turn or random coil. Most models contain parameters for the likelihood of helix nucleation from a coil region, and helix propagation along the sequence once nucleated; because polypeptides are directional and have distinct N-terminal and C-terminal ends, propagation parameters may differ in each direction.

Common transition models include the Zimm-Bragg model and the Lifson-Roig model, and their extensions and variations.

Energy of host poly-alanine helix in the aqueous solution:

ΔGfolding = (m − 2)ΔHαmTΔS

where m - is number of residues in the helix [1]


  1. ^ Chakrabartty, A., Baldwin, R.L. 1995. Stability of alpha-helices. Adv. Protein Chem.,46:141-176.
This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Helix-coil_transition_model". A list of authors is available in Wikipedia.
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