Helix-coil transition in homopolypeptides under stretching.

We consider the effect of an external applied force on the alpha-helix-coil transition of a single-stranded homopolypeptide chain. An annealed scenario is assumed, where the building amino acid monomers may interconvert between random-coiled and ordered alpha-helical configurations. By exact evaluation of the partition function of the freely jointed chain with helix-coil internal degrees of freedom in the thermodynamic limit, we obtain the result that the stress-strain characteristic has an asymmetrical sigmoid shape with a prominent pseudoplateau. Because of the one-dimensional nature of this system, fluctuations dominate over the mean-field approximation, which incorrectly predicts a second-order phase transition.