Cel
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.
Dziedzina nauki
- natural sciencesbiological sciencesneurobiology
- medical and health sciencesbasic medicinemedicinal chemistry
- natural sciencescomputer and information sciencescomputational science
- natural sciencesphysical sciencesopticsspectroscopyabsorption spectroscopy
- natural sciencesbiological sciencesbiochemistrybiomoleculesproteinsenzymes
Zaproszenie do składania wniosków
FP7-PEOPLE-2009-IOF
Zobacz inne projekty w ramach tego zaproszenia
System finansowania
MC-IOF - International Outgoing Fellowships (IOF)Koordynator
NE1 8ST Newcastle Upon Tyne
Zjednoczone Królestwo