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CoHSI I; Detailed properties of the Canonical Distribution for Discrete Systems such as the Proteome

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 Added by Les Hatton
 Publication date 2018
  fields Biology
and research's language is English




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The CoHSI (Conservation of Hartley-Shannon Information) distribution is at the heart of a wide-class of discrete systems, defining the length distribution of their components amongst other global properties. Discrete systems such as the known proteome where components are proteins, computer software, where components are functions and texts where components are books, are all known to fit this distribution accurately. In this short paper, we explore its solution and its resulting properties and lay the foundation for a series of papers which will demonstrate amongst other things, why the average length of components is so highly conserved and why long components occur so frequently in these systems. These properties are not amenable to local arguments such as natural selection in the case of the proteome or human volition in the case of computer software, and indeed turn out to be inevitable global properties of discrete systems devolving directly from CoHSI and shared by all. We will illustrate this using examples from the Uniprot protein database as a prelude to subsequent studies.

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90 - Les Hatton , Gregory Warr 2018
The CoHSI (Conservation of Hartley-Shannon Information) distribution is at the heart of a wide-class of discrete systems, defining (amongst other properties) the length distribution of their components. Discrete systems such as the known proteome, computer software and texts are all known to fit this distribution accurately. In a previous paper, we explored the properties of this distribution in detail. Here we will use these properties to show why the average length of components in general and proteins in particular is highly conserved, howsoever measured, demonstrating this on various aggregations of proteins taken from the UniProt database. We will go on to define departures from this equilibrium state, identifying fine structure in the average length of eukaryotic proteins that result from evolutionary processes.
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