University of the Western Cape
PhD/Postdoc in Phage Display
A PhD/Postdoc position is available in the Protein-protein
Interaction group at the University of the Western Cape to implement
a Phage Display screen1 for
the identification of novel protein-protein interactions. The group
currently comprises 4 PhD and 2 MSc students, focussing primarily on
interactions involving the RBBP6 p53-associated protein2;
3. The project will complement a number of similar
techniques currently in use within the group, including yeast
two-hybrid, immunoprecipitation, BIACore and NMR-based studies. The
group has excellent facilities for molecular biology and bacterial
protein expression, BIACore and fluorescence microscopy, as well as
access to a 600 MHz NMR spectrometer configured for biomolecular
work at a nearby institution.
The University of the Western Cape is situated 20 minutes’ drive
from central Cape Town. Cape Town and the surrounding areas offer
excellent quality of life, including mountains, beaches, winelands
and fine restaurants. Childcare and excellent schools are readily
available.
Applicants should have a strong background in molecular biology.
Previous experience of phage display or the construction of cDNA
libraries would be an advantage, but are not essential.
For more information contact Dr David Pugh, email:
dpugh@uwc.ac.za. To apply, send
a covering letter, a CV containing details of previous courses and
associated grades and the email addresses of 3 referees to the above
address.
More information:
1. Lanzillotti, R. & Coetzer, T. L. (2008). Phage display: a
useful tool for malaria research? Trends Parasitol 24, 18-23.
Pubmed
2. Pugh, D. J., AB, E., Faro, A., Lutya, P. T., Hoffmann, E. & Rees,
D. J. (2006). DWNN, a novel ubiquitin-like domain, implicates RBBP6
in mRNA processing and ubiquitin-like pathways. BMC Struct Biol 6,
1.
Pubmed
3. Chibi, M., Meyer, M., Skepu, A., Rees, D. J., Moolman-Smook, J.
C. & Pugh, D. J. (2008). RBBP6 Interacts with Multifunctional
Protein YB-1 through Its RING Finger Domain, Leading to
Ubiquitination and Proteosomal Degradation of YB-1. J Mol Biol.
Pubmed
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