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Size dependent complexity of sequences in protein families

J. Li, J. Wang and W. Wang ()

The European Physical Journal B: Condensed Matter and Complex Systems, 2005, vol. 47, issue 3, 431-436

Abstract: The size dependent complexity of protein sequences in various families in the FSSP database is characterized by sequence entropy, sequence similarity and sequence identity. As the average length L f of sequences in the family increases, an increasing trend of the sequence entropy and a decreasing trend of the sequence similarity and sequence identity are found. As L f increases beyond 250, a saturation of the sequence entropy, the sequence similarity and the sequence identity is observed. Such a saturated behavior of complexity is attributed to the saturation of the probability P g of global (long-range) interactions in protein structures when L f >250. It is also found that the alphabet size of residue types describing the sequence diversity depends on the value of L f , and becomes saturated at 12. Copyright EDP Sciences/Società Italiana di Fisica/Springer-Verlag 2005

Date: 2005
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DOI: 10.1140/epjb/e2005-00333-x

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