Thermodynamics of helix-coil transitions studied by multicanonical algorithms

Details Thermodynamics of helix-coil transitions studied by multicanonical algorithms Thermodynamics of helix-coil transitions studied by multicanonical algorithms

1995-05-25

arxiv.org/abs/chem-ph/9505006v1

Physics

Chemical Physics

35 pages, no figures included; to appear in J.Phys.Chem

Scientific paper

Thermodynamics of helix-coil transitions in amino-acid homo-oligomers are studied by the recently proposed multicanonical algorithms. Homo-oligomers of length 10 are considered for three characteristic amino acids, alanine (helix former), valine (helix indifferent), and glycine (helix breaker). For alanine other lengths (15 and 20) are also considered in order to examine the length dependence. From one multicanonical production run with completely random initial conformations, we have obtained the lowest-energy conformations and various thermodynamic quantities (average helicity, Zimm-Bragg $s$ and $\sigma$ parameters, free energy differences between helix and coil states, etc.) as functions of temperature. The results confirm the fact that alanine is helix-forming, valine is helix-indifferent, and glycine is helix-breaking.

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