---- Original message ----
>Date: Thu, 19 Jul 2007 16:29:18 -0400
>From: Michel_Dumontier <[EMAIL PROTECTED]>
>Subject: RE: protein entities (was Re: Rules (was Re: Ambiguous names. was:
>Re: URL +1, LSID -1)
>To: Darren Natale <[EMAIL PROTECTED]>, Michel_Dumontier <[EMAIL PROTECTED]>
>Cc: Eric Jain <[EMAIL PROTECTED]>, Alan Ruttenberg <[EMAIL PROTECTED]>, Chris
>Mungall <[EMAIL PROTECTED]>, Bijan Parsia <[EMAIL PROTECTED]>,
>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)in 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
