Abstract
Abstract We report the results of multicanonical simulations on α-helix propensities of homo-oligomers of nonpolar amino acids. Three characteristic amino acids are considered: alanine (helix former), glycine (helix breaker), and valine (helix indifferent). Starting simulations from completely random initial conformations, we have calculated the average % helix, free energy differences of helix-coil transitions, and the Zimm-Bragg s parameters over a wide range of temperatures. The results are shown to be in good agreement with experiments.
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