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As evidenced by a buried core of hydrophobic residues within globular proteins, hydrophobicity provides essential insights into the folding structure of proteins. Previous studies have shown that hydrophobic residues show statistically meaningful distribution on the primary sequence, but most of them lacked further investigation into a potential relationship to secondary structure elements. In this...
Eight representative physicochemical properties of amino acids are considered to encode each residue and correlative information is examined in relation to the formation of protein secondary structure. Features salient at the coarse level are first gleaned through vector quantization technique and then more refined class-specific features are identified based on the vector element-wise analysis. Effectiveness...
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