Received: by alpheratz.cpm.aca.mmu.ac.uk id MAA20717 (8.6.9/5.3[ref firstname.lastname@example.org] for cpm.aca.mmu.ac.uk from email@example.com); Mon, 20 Aug 2001 12:08:54 +0100 Message-ID: <3B80EF02.12BBE238@bioinf.man.ac.uk> Date: Mon, 20 Aug 2001 12:05:38 +0100 From: Chris Taylor <Christopher.Taylor@man.ac.uk> Organization: University of Manchester X-Mailer: Mozilla 4.77 [en] (Windows NT 5.0; U) X-Accept-Language: en To: firstname.lastname@example.org Subject: Re: Multiple-minimum References: <3B7C1628.32445.5EAA81@localhost> <008301c128fb$d68928e0$c024f4d8@teddace> Content-Type: text/plain; charset=iso-8859-1 Content-Transfer-Encoding: 8bit Sender: email@example.com Precedence: bulk Reply-To: firstname.lastname@example.org
> 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 (email@example.com)
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