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In the present paper we present results of calculations obtained
with the use of the theoretical method described in our preceding
paper [Eur. Phys. J. D, DOI: 10.1140/epjd/e2007-00328-9] and perform detail analysis of
α-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 [Eur. Phys. J. D, DOI: 10.1140/epjd/e2007-00328-9].
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
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