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Structure and mechanism of a pyridoxal-dependent transaminase ribozyme
Reference
BB/C514582/1
Principal Investigator / Supervisor
Professor David Hodgson
Co-Investigators /
Co-Supervisors
Institution
Durham University
Department
Chemistry
Funding type
Research
Value (£)
187,496
Status
Completed
Type
Research Grant
Start date
01/10/2005
End date
30/09/2008
Duration
36 months
Abstract
A pyridoxamine-dependent transaminase ribozyme that has been isolated through in vitro selection will be studied in detail. Product analysis studies using isotope labelling and/or nanospray-LC-FT-ICR-ESMS will be performed in order to cofirm this transaminase activity using a number of potential substrates. The substrate preferences and general kinetic properties of the ribozyme will be determined using a gel shift assay. The tertiary structure of the ribozyme will be determined using mutant ribozymes, nuclease, chemical modification and metal ion mapping techniques along with photo-cross-linking studies in order to confirm the tertiary structure. Nucleotide analogue interference mapping (NAIM) will be used to determine the catalytic roles of individual functional groups within the ribozyme.
Summary
unavailable
Committee
Closed Committee - Biomolecular Sciences (BMS)
Research Topics
Structural Biology
Research Priority
X – Research Priority information not available
Research Initiative
X - not in an Initiative
Funding Scheme
X – not Funded via a specific Funding Scheme
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