Professor Helen J. Cooper PhD FRSC

BSc (Hons) Chemistry, University of Warwick

PhD Chemistry, University of Warwick

Professor Helen J. Cooper obtained her BSc and PhD in Chemistry at the University of Warwick. She began her post-doctoral career at the University of Warwick, before taking a faculty position at the National High Magnetic Field Laboratory, Florida State University, in 2000. In 2003, she returned to the UK as Wellcome Trust Value-in-People Fellow at the University of Birmingham.She was subsequently awarded a Wellcome Trust University Technology Fellowship to develop high performance mass spectrometry methods for use in biomedical research. In 2010, she took up the post of Senior Lecturer.

Professor Cooper teaches at both undergraduate (1st, 2nd and final year) and postgraduate (MSc, MRes) level. She is committed to research-informed teaching and enquiry-based learning. She is currently undertaking the Postgraduate Certificate in Learning & Teaching in Higher Education.

For a list of possible PhD projects offered by Professor Cooper www.findaphd.com/search/customlink.asp?inst=birm-Biol&supersurname=Cooper

Research Theme within School of Biosciences: Molecular and Cell Biology

Cooper Mass spectrometry group web site 

Advanced mass spectrometry techniques for the analysis of biomolecular and chemical structure

We are interested in the development and application of mass spectrometry techniques for the characterisation of biomolecular and non-biomolecular structures. Current work in the laboratory focuses on the following areas:

Thermo Fisher LTQ FT Ultra mass spectrometer

1. Development of methods for proteomics Proteomics involves the study of the entire protein complement of a cell or system. In bottom-up proteomics, proteins are digested and the resulting peptides are analysed by liquid chromatography tandem mass spectrometry. The aim is to identify, characterise and quantify the peptides and hence proteins. We are developing methods for proteomics using Fourier transform mass spectrometry together with electron capture dissociation (ECD), electron transfer dissociation (ETD) and collision induced dissociation (CID).

2. Fundamentals of peptide fragmentation Peptide fragmentation is central to the field of proteomics. Peptide fragmentation provides sequence information which in turn enables protein identification. In order to obtain as much information as possible about a peptide, it is necessary to fully understand the mechanisms by which it fragments in the mass spectrometer. We apply a model peptide approach to investigate the fundamentals of peptide fragmentation. We are particularly interested in the mechanisms of electron capture/transfer dissociation.

Thermo Fisher Orbitrap Velos ETD with FAIMS

3. Analysis of post-translational modifications Structural elucidation of post-translationally modified peptides and proteins is of key importance in the understanding of an array of biological processes. For example, protein phosphorylation is a key event in signal transduction. Full insight into signalling processes requires identification of modified proteins and determination of the exact sites of modification. Modifications studied include phosphorylation, ubiquitination, nitration, glycosylation and citrullination.

4. Ion mobility spectrometry and mass spectrometry Post-translational modifications alter local interactions and hence the overall structure of a protein. Ion mobility spectrometry separates ions on the basis of their shape (and charge) whereas mass spectrometry separates ions on the basis of their mass (and charge). We are developing methods which exploit ion mobility for the analysis of post-translational modifications.

5. Direct surface sampling of dried blood spots In collaboration with Birmingham Children’s Hospital, we are developing mass spectrometry-based methods for the diagnosis of inherited disorders in newborns.