  In the present paper we present results of calculations obtained with the use
of the theoretical method described in our preceding paper [1] and perform
detail analysis of alpha helix-random coil transition in alanine polypeptides
of different length. We have calculated the potential energy surfaces of
polypeptides with respect to their twisting degrees of freedom and construct a
parameter-free partition function of the polypeptide using the suggested method
[1]. From the build up partition function we derive various thermodynamical
characteristics for alanine polypeptides of different length as a function of
temperature. Thus, we analyze the temperature dependence of the heat capacity,
latent heat and helicity for alanine polypeptides consisting of 21, 30, 40, 50
and 100 amino acids. Alternatively, we have obtained same thermodynamical
characteristics from the use of molecular dynamics simulations and compared
them with the results of the new statistical mechanics approach. The comparison
proves the validity of the statistical mechanic approach and establishes its
accuracy.
