Distances and classification of amino acids for different protein secondary structures

Physics – Biological Physics

Scientific paper

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15 pages, 8 figures

Scientific paper

10.1103/PhysRevE.67.051927

Window profiles of amino acids in protein sequences are taken as a description of the amino acid environment. The relative entropy or Kullback-Leibler distance derived from profiles is used as a measure of dissimilarity for comparison of amino acids and secondary structure conformations. Distance matrices of amino acid pairs at different conformations are obtained, which display a non-negligible dependence of amino acid similarity on conformations. Based on the conformation specific distances clustering analysis for amino acids is conducted.

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