Switzerland,PhD position in Biochemistry/Molecular Biology

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Retinal is the photon coupling cofactor of rhodopsin in the photoreceptors of the bearcat eye retina. The photon apprenticed cis-trans isomerization of the 11-cis-retinal triggers a avalanche of signaltransduction reactions amplifying the arresting and eventually consistent in the beheld response. Once isomerized 11-trans-retinal is no best alive and charge be exchanged for beginning 11-cis-retinal. Persistent eyes in vertebrates accordingly depends on the connected regene allowance of 11-cis-retinal from all-trans-retinal. This about-face is a multistep acknowledgment alleged the beheld cycle. The enzymes of this aeon are broadcast amid photo re ceptor beef and adjoining retinal colorant epithelium (RPE) cells.

CRALBP, the cellular retinaldehyde-binding protein, chaperones the acknowledgment intermediates of the RPE amid the regenerating enzymes and prevents abortive cis-trans isomerization. It possesses a aerial affection 11-cis-retinoid bounden abridged and forms protein-protein complexes with the film protein 11-cis-retinol dehydrogenase (RDH5) and possibly is circuitous in the accumulation of a retinoid-processing film protein circuitous of the RPE. Dysfunction of CRALBP has been associated with a cardinal of astringent retinopathies.

Thesis Project: In this PhD apriorism project, we adduce to analyze the mechanisms that underlie the connected regene allowance of 11-cis-retinal from all-trans-retinal by the retinoid-processing film protein circuitous of the RPE including CRALBP and its ache causing mutants. We aim at the compassionate the 3D anatomy of CRALPB and the structural alterations in clinically accordant mutants as prerequisite for a atomic account of the beheld cycle’s function, assertive of its pathologies and for advance appear their therapy. Furthermore we aim at the spectroscopic assuming of the retinoid-processing film protein circuitous in RPE beef and its decision by electron microscopy. Specific aims of this analysis activity are: (i) X-ray anatomy of clinically accordant CRALBP mutants and quantitative in vitro assuming of retinoid ligand binding. (ii) Assuming of retinoid-processing film protein complexes. We apply X-ray crystallography, site-directed mutagenesis, spectroscopic and electron diminutive methods in adjustment to acquire structure-function relationships.
Application Deadline 1 September 2010

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