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Détails de cette annonce:
De: Stefan Szedlacsek, le Mardi 02/01/2007
Département/Pays: Bucarest, ROUMANIE
I am writing you kindly asking your help in advertising among the members of your Society of an open PhD student position in my lab. Personally, I am confident about the high potential of the biochemistry in your country and that is why I hope that promissing candidates from Maroc could be interested in this PhD student position. I am attaching here the text of the advertisment.
Thank you very much in advance and, as we are at the beginning of 2007, I would like to take this opportunity and wish you a very Happy New Year!
Stefan Szedlacsek, Phd
Professor of Biochemistry
Head, Department of Enzymology
Institute of Biochemistry
of the Romanian Academy
Spl. Independentei 296
Application for PhD Programme in structural biology and enzyme kinetics
Applications are welcomed for a PhD student position in the Department of Enzymology at the Institute of Biochemistry of the Romanian Academy of Sciences from Bucharest (Romania). This position is funded under a new FP6 Marie Curie Research Training Network - “PTPNET”. The Network contains twelve research teams and will focus in depth on protein tyrosine phosphatase (PTP) structure, regulation and function. This Network will be highly collaborative in nature, providing exciting opportunities for researchers to work in several disciplines and to be exposed to both academia and industry.
The team leader of the Romanian group is Professor Stefan Szedlacsek. The specific interest of the group is to understand the structure-function relationships of PTPs and the possible relevance for their physiological role. Using an enzyme kinetic approach, this group has so far obtained important results concerning the interrelationship between intracellular regions of PTPµ. In addition, the group crystallized and solved (in a highly successful international collaboration) the corresponding crystal structure of PTP-SL/BR7 - the first structure of a receptor-like PTP with a single cytoplasmic domain. Given the unique expertise of the group in enzymatic analysis (particularly enzyme kinetics) as well as their structural biology experience, the group provides the main Network expertise in enzyme kinetics, screening facilities for substrate specificity analysis as well as tools for structural analysis of the intracellular regions of PTPs.
Two main goals are set for this PhD project. First: to determine the 3D-crystal structure of non-catalytic cytoplasmic subdomains of PTPs. Second: to evaluate the substrate specificities and determine the effects of specific modulators and mutations on the enzymatic activity of PTPs. It is also intended to perform correlation analysis between structural and activity data thus obtained. Modern experimental procedures will be applied, like recombinant DNA technologies, protein expression, protein purification and crystallization, spectroscopy, enzyme kinetics analysis. The successful PhD student will be given intensive Network training through dedicated workshops and will be given opportunities to work with other teams during secondments.
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