Via: UK.AC.ABERYSTWYTH; Tue, 28 May 91 17:28 WET (V40 at
UK.AC.DARESBURY.DLGM)
Received:by uk.ac.aber.aberda (5.57/aberclient-4.0) id AA06766; Tue, 28 May 91
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Message-Id: <9105281632.AA06766 at uk.ac.aber.aberda>
To: biosci at uk.ac.daresbury
Cc: edt at uk.ac.aber
Subject: Protein conformation and primary sequence revisited ?
Date: Tue, 4 Jun 91 08:56 GMT
From: edt at uk.ac.aber
Being a rather naive microbial physiologist it was interesting to hear from
Dr Gwyn Gould (Molecular Pharmacology Group, Dept. of Biochemistry, University
of Glasgow, UK) that five facilitative glucose transporters (from rat tissue)
would appear to share a 50-55% primary sequence homology in the transmembrane
sections of their structures. Each transporter folding into a similar native
conformation in these regions (12 alpha helices). Considering each transporter
exhibits distinct kinetic characteristics and are the products of genes
resident on separate chromosomes, surely this should enable some progress in
the rationalization of defining a correlation between protein primary
structure and gross conformation ?
