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Dear ammrlers,
I have been asked to post this advert. Apologies for cross-posting
University of Birmingham, School of Biochemistry.
Post-doctoral research fellow - NMR spectroscopist.
Post-doctoral research fellow is required to examine the structure and dyna=
mics of a 7=20
kDa peptide, which is an inhibitor of platelet aggregation and adhesion, an=
d selected=20
mutants. Experience in NMR spectroscopy, or structure determination from NM=
R=20
constraints, is essential.=20
The position is funded by the British Heart Foundation from 1st January for=
two years=20
with a salary in the RA1A scale, =A3 15,735- 22,726 p.a.=20
Informal enquiries to Dr Eva I Hyde, email e.i.hyde@bham.ac.uk, Tel 0121-41=
4-5393.=20
Further particulars and applications forms from the Director of Staffing se=
rvices,=20
University of Birmingham, Edgbaston, Birmingham, B15 2TT. Tel 0121-414-7044=
,=20
email STAFFING@bham.ac.uk, web http://www.bham.ac.uk/staffing.=20
Reference S35177/98.=20
Further particulars:
University of Birmingham, School of Biochemistry,
Research Fellow - NMR spectroscopist.
This post-doctoral position is for an NMR spectroscopist to examine the str=
ucture and=20
dynamics of a 7 kDa neurotoxin homologue, dendroaspin, which acts as a pote=
nt=20
inhibitor of platelet aggregation and adhesion. The project is a collaborat=
ion between=20
Dr Eva Hyde at the School of Biochemistry, University of Birmingham, and Dr=
=2E Xinjie=20
Lu at the Thrombosis Research Institute, London. The peptide, originally is=
olated from=20
snake toxin, has been cloned into an expression vector and expressed in E. =
coli. This=20
allows preparation of 15N-labelled protein for dynamic studies and also pre=
paration of=20
site specific mutants. We have previously determined the structure of the w=
ild type=20
protein, [Sutcliffe et al., (1994) Nature Structural Biology, 1, 802-807] a=
nd of another=20
peptide from snake venom that has the same function but a different structu=
re,=20
albolabrin [Smith et al, ( 1996) Int. J. Peptide Protein Res, 48, 220-228].=
Comparison=20
of the two structures suggests that the key feature for activity may be the=
presence of=20
an RGD-motif at the end of a flexible loop. The postdoctoral fellow, to be =
based in=20
Birmingham, will examine the dynamics of the peptide using 15N-relaxation=
=20
measurements and also the structures of dendroaspin mutants with changes in=
a second=20
motif, which may affect the structure of the peptide.
The University has good facilities for biological NMR studies, including a =
Bruker=20
AMX 500 and a Varian Unityplus 600 NMR spectrometer, both with three channe=
ls=20
and pulsed z-field gradients. It has excellent computing equipment, partly =
funded by an=20
MRC infrastructure award in 'Bioinformatics and Structural Analysis' and th=
e Glaxo-
Wellcome Biocomputing laboratory has just been inaugurated. There is a sepa=
rate=20
Silicon Graphics Iris Indigo in EIH's laboratory networked to the NMR and=
=20
biocomputing facilities. EIH's group is involved in other NMR projects and =
there are=20
close contacts to other groups in the University using NMR spectroscopy, X-=
ray=20
crystallography, modelling, and other biophysical techniques to study struc=
ture-
function relationships in proteins.
Applicants should have, or be about to obtain, a PhD in Biochemistry, Chemi=
stry or a=20
related subject. Experience of NMR spectroscopy or of structural calculatio=
ns from=20
NMR constraints is essential, preferably as applied to proteins. An interes=
t in protein=20
design and mutagenesis would be an advantage. The position is funded by the=
British=20
Heart Foundation to point 10 of the RA1A scale (with 2 point increment) for=
2 years,=20
from 1st January, 1999. Informal enquiries should be addressed to Dr Eva Hy=
de, email=20
e.i.hyde@bham.ac.uk; Tel:0121-414-5393.=20
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