---- Original message ----
>Date: Thu, 19 Jul 2007 16:29:18 -0400
>From: Michel_Dumontier <Michel_Dumontier carleton.ca>
>Subject: RE: protein entities (was Re: Rules (was Re:
Ambiguous names. was: Re: URL +1, LSID -1)
>To: Darren Natale <dan5 georgetown.edu>,
Michel_Dumontier <Michel_Dumontier carleton.ca>
>Cc: Eric Jain <Eric.Jain isb-sib.ch>, Alan
Ruttenberg <alanruttenberg gmail.com>, Chris
Mungall <cjm fruitfly.org>, Bijan Parsia
<bparsia cs.man.ac.uk>, public-semweb-lifesci hcls
<public-semweb-lifesci w3.org>
>
>
>Darren,
>
>> Also, while we recognize
>> that there are different qualities that can be
ascribed to a basically
>> identical biochemical entity in different
structural conformations or
>> states of ligand binding, we are not attempting (at
least in the
>> beginning) to describe these structural
conformations or bound vs
>> unbound forms.
>
>Indeed, while conformation is an important quality of
molecular
>structure, it does not fundamentally change the nature
of the molecule.
>i.e. a protein in a bound or unbound state should still
be considered
>the same protein.
>
>Cheers,
>
>-=Michel=-
>
>
Many post-translational modifications like glycosylation (http://www.functionalglycomics.org/static/index.shtml)i
n proteins fundamentally change the (functional) 'nature' of
the protein (as also the molecular structure of the protein
in case of glycosylation through addition of sugar chains
(glycans)).
Satya Sahoo
Knoesis Center
http://knoesis.wright.edu
a>
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