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EXPLORING PROTEIN'S OPTIMAL HP CONFIGURATIONS BY SELF-ORGANIZING MAPPING

    Self-organizing map (SOM) has been used in protein folding prediction when the HP model is employed. The existing work uses a square-like shape lattice with l = m×n points to represent the optimal compact structure of a sequence of l amino acids. In this paper, a general l′-size sequence of amino acids is self-organized in a two dimensional lattice with l (> l′) points. The obtained minimum configuration then has a flexible shape, in contrast to the compact structure limited in the lattice. To fulfil this extension, a new self-organizing map (SOM) technique is proposed to deal with the difficulty of the unsymmetric input and output spaces. New competition rules in the training phase are introduced and a local search method is applied to overcome the multi-mapping phenomena. Several HP benchmark examples with up to 36 amino acids are tested to verify the effectiveness of the proposed approach in this paper.

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