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Content archived on 2024-05-27

An Integrated Computational and Spectroscopic Investigation of the Enzyme Mechanism of Tryptophan Hydroxylase

Objective

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.

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Topic(s)

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Call for proposal

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FP7-PEOPLE-2009-IOF
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Funding Scheme

Funding scheme (or “Type of Action”) inside a programme with common features. It specifies: the scope of what is funded; the reimbursement rate; specific evaluation criteria to qualify for funding; and the use of simplified forms of costs like lump sums.

MC-IOF - International Outgoing Fellowships (IOF)

Coordinator

UNIVERSITY OF NORTHUMBRIA AT NEWCASTLE
EU contribution
€ 334 689,80
Address
SUTHERLAND BUILDING COLLEGE STREET
NE1 8ST NEWCASTLE UPON TYNE
United Kingdom

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Region
North East (England) Northumberland and Tyne and Wear Tyneside
Activity type
Higher or Secondary Education Establishments
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Total cost

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