I am posting this vacancy on behalf of Dr. Eva Hyde. Please
forgive cross-postings.
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University of Birmingham, School of Biochemistry.
Post-doctoral research fellow - NMR spectroscopist.
Post-doctoral research fellow is required to examine the structure and dynamics of a 7
kDa peptide, which is an inhibitor of platelet aggregation and adhesion, and selected
mutants. Experience in NMR spectroscopy, or structure determination from NMR
constraints, is essential.
The position is funded by the British Heart Foundation from 1st January for two years
with a salary in the RA1A scale, £ 15,735- 22,726 p.a.
Informal enquiries to Dr Eva I Hyde, email e.i.hyde@bham.ac.uk, Tel 0121-414-5393.
Further particulars and applications forms from the Director of Staffing services,
University of Birmingham, Edgbaston, Birmingham, B15 2TT. Tel 0121-414-7044,
email STAFFING@bham.ac.uk, web http://www.bham.ac.uk/staffing.
Reference S35177/98.
Closing date Nov 5th.
Further particulars:
University of Birmingham, School of Biochemistry,
Research Fellow - NMR spectroscopist.
This post-doctoral position is for an NMR spectroscopist to examine the structure and
dynamics of a 7 kDa neurotoxin homologue, dendroaspin, which acts as a potent
inhibitor of platelet aggregation and adhesion. The project is a collaboration between
Dr Eva Hyde at the School of Biochemistry, University of Birmingham, and Dr. Xinjie
Lu at the Thrombosis Research Institute, London. The peptide, originally isolated from
snake toxin, has been cloned into an expression vector and expressed in E. coli. This
allows preparation of 15N-labelled protein for dynamic studies and also preparation of
site specific mutants. We have previously determined the structure of the wild type
protein, [Sutcliffe et al., (1994) Nature Structural Biology, 1, 802-807] and of another
peptide from snake venom that has the same function but a different structure,
albolabrin [Smith et al, ( 1996) Int. J. Peptide Protein Res, 48, 220-228]. Comparison
of the two structures suggests that the key feature for activity may be the presence of
an RGD-motif at the end of a flexible loop. The postdoctoral fellow, to be based in
Birmingham, will examine the dynamics of the peptide using 15N-relaxation
measurements and also the structures of dendroaspin mutants with changes in a second
motif, which may affect the structure of the peptide.
The University has good facilities for biological NMR studies, including a Bruker
AMX 500 and a Varian Unityplus 600 NMR spectrometer, both with three channels
and pulsed z-field gradients. It has excellent computing equipment, partly funded by an
MRC infrastructure award in ‘Bioinformatics and Structural Analysis’ and the Glaxo-
Wellcome Biocomputing laboratory has just been inaugurated. There is a separate
Silicon Graphics Iris Indigo in EIH’s laboratory networked to the NMR and
biocomputing facilities. EIH’s group is involved in other NMR projects and there are
close contacts to other groups in the University using NMR spectroscopy, X-ray
crystallography, modelling, and other biophysical techniques to study structure-
function relationships in proteins.
Applicants should have, or be about to obtain, a PhD in Biochemistry, Chemistry or a
related subject. Experience of NMR spectroscopy or of structural calculations from
NMR constraints is essential, preferably as applied to proteins. An interest in protein
design and mutagenesis would be an advantage. The position is funded by the British
Heart Foundation to point 10 of the RA1A scale (with 2 point increment) for 2 years,
from 1st January, 1999. Informal enquiries should be addressed to Dr Eva Hyde, email
e.i.hyde@bham.ac.uk; Tel:0121-414-5393.
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Regards,
Tony Pemberton
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Mr. A.J.Pemberton Tel: +121-414-3388
c/o Dept. Rheumatology, Fax: +121-414-3982
Medical School, E-mail: A.J.Pemberton@bham.ac.uk
The University of Birmingham,
Birmingham B15 2TT.
U.K.
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