Objetivo
Metalloenzymes play crucial role in neurobiology and therefore they are very important target for drug design for treatment neuropathological processes. In order to make new specific and effective drugs it is crucially important to understand the structure and functions of their drug targets. In this Outgoing Marie Curie Fellowship application we propose combined computational/spectroscopic investigation of the enzyme mechanism of tryptophan hydroxylase – a pterin-dependent non-heme containing iron enzyme in crucial importance for the nervous system. Accurate insight in the mechanism of such a complicated enzyme can not be received using solely computational or experimental methods therefore we will apply integrated combination of state-of-the-art computational methods with most modern spectroscopy methods (e.g. K edge X-ray Absorption Spectroscopy, Magnetic Circular Dichroism and variable-temperature variable-field MCD, and EPR). The results will provide understanding of the structure-functions relationships of this enzyme and will be used in drug design.
Ámbito científico
- natural sciencesbiological sciencesneurobiology
- medical and health sciencesbasic medicinemedicinal chemistry
- natural sciencescomputer and information sciencescomputational science
- natural sciencesphysical sciencesopticsspectroscopyabsorption spectroscopy
- natural sciencesbiological sciencesbiochemistrybiomoleculesproteinsenzymes
Convocatoria de propuestas
FP7-PEOPLE-2009-IOF
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Régimen de financiación
MC-IOF - International Outgoing Fellowships (IOF)Coordinador
NE1 8ST Newcastle Upon Tyne
Reino Unido