Path: utzoo!utgpu!news-server.csri.toronto.edu!rpi!zaphod.mps.ohio-state.edu!wuarchive!uwm.edu!bionet!dlgm.daresbury.ac.uk!SEQ From: SEQ@dlgm.daresbury.ac.uk (DARESBURY SEQMAIL) Newsgroups: bionet.molbio.proteins Subject: (none) Message-ID: <04.JUN.1991.08:56:43.SEQ@UK.AC.DARESBURY.DLGM> Date: 4 Jun 91 08:56:00 GMT Sender: daemon@genbank.bio.net Distribution: bionet Lines: 22 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 17:32:29 +0100 Message-Id: <9105281632.AA06766@uk.ac.aber.aberda> To: biosci@uk.ac.daresbury Cc: edt@uk.ac.aber Subject: Protein conformation and primary sequence revisited ? Date: Tue, 4 Jun 91 08:56 GMT From: edt@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 ?