Evolution of proteins in sequence space

From: pruest@pop.dplanet.ch
Date: Fri Aug 17 2001 - 11:05:09 EDT

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    Wayne,

    thank you for your detailed description of the persistence length in
    polypeptides and its relevance for evolution moving around in sequence
    space (13 Aug 2001 12:29:31 EDT). I'll be glad to look at your upcoming
    paper in J.theoret.Biol.

    The important reduction of possible sequences from L^20 to perhaps
    (L/3)^(8..10) indicates that the vast majority of codon sequences
    produced by random mutational walks will not specify physically possible
    proteins, let alone functional ones. Presumably after (or even during)
    translation, such a protein, being unable to fold up, will be degraded,
    and the new mutation generating it will be discarded immediately.

    This sparsity of viable proteins in sequence space accords with the
    finding (which I discussed before) that even for simple partial
    functions the vast majority of randomly generated polypeptides is
    inactive (not more than 1 in 10^11 is active for ATP binding).

    Peter 

    -- 
Dr Peter Ruest, <pruest@dplanet.ch>
CH-3148 Lanzenhaeusern, Switzerland
Biochemistry - Creation and evolution
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Creative providence in biology (Gen.2:3):
"..the work which God created (in order) to (actively) evolve it"
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