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Proteomics is functional genomics at the
protein level – that is, the study of protein properties (such as
expression level, post-translational modification, interactions, etc.)
on a global scale to obtain a integrated view of disease processes,
cellular processes and networks at the protein level. Originally part
of the Third Generation Proteomics (3GP) Programme, my research aims to
develop and advance our mass spectrometric capabilities for the
characterisation of intact proteins and protein/protein complexes, and
the identifiability of post-translational modifications and
protein/protein interactions. Core to this is the application of a
Fourier Transform Ion Cyclotron Resonance (FT-ICR) Mass Spectrometer .
This instrument offers mass resolving powers and mass accuracy orders
of magnitude better than conventional mass spectrometers. It also
allows molecular ions (proteins and peptides, in the context of the 3GP
programme), to be selectively trapped and manipulated over extended
periods allowing both time and energy resolved gas-phase reactions to
be employed.
My doctoral work was mainly focused on investigation of nanostructures
My role within the research group centres on the development of
experimental methods and the provision of access to a range of
techniques and experimental configurations for projects requiring the
specific capabilities of the FT-ICR mass spectrometer. The scope of my
work ranges from metabolites and small pharmaceutical compounds to
intact proteins and post-translational modifications. Collaborations
benefitting from FT-ICR MS include the Bioanalytical Sciences Group,
the Leukaemia Research Fund, and Jane Thomas-Oates Mass Spectrometry
Group at the University of York .
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