Re: Multiple-minimum

From: Chris Taylor (Christopher.Taylor@man.ac.uk)
Date: Mon Aug 20 2001 - 12:05:38 BST

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Date: Mon, 20 Aug 2001 12:05:38 +0100
From: Chris Taylor <Christopher.Taylor@man.ac.uk>
Organization: University of Manchester
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Subject: Re: Multiple-minimum
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    > According to morphic theory, the same protein configuration should occur
    > even when composed of entirely different sequences of amino acids. This is
    > exactly what happens. Among the serine proteases, for instance, only 40% of
    > the positions in the polypeptide chains are occupied by the same amino
    > acids. Yet they are strikingly similar, with most of the twists and turns
    > being identical. Same thing with the hemoglobins. They all have virtually
    > the same structure, yet none of them share more than three amino acids out
    > of the 140 to 150 slots along the chain.

    My entire Ph.D. was on neutral evolution - there are many peptides that
    fold to the same protein (same with RNA secondary structures). This
    works both ways too - striking similar sequences can do radically
    different jobs when folded and in situ. However none of this remotely
    challenges the existing orthodoxy about protein folding, or evolution.
    If MR were true, then why is such neutral drift allowed? (The novelty
    problem *again* - not answered so far).

    ~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~
     Chris Taylor (chris@bioinf.man.ac.uk)
     http://bioinf.man.ac.uk/ »people»chris
    ~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~~

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