*Information obtained from http://www.liv.ac.uk/pfg

Professor Rob Beynon BSc PhD

"My main areas of research are in the areas of protein chemistry, proteomics, proteolysis, and proteolytic enzymes, with emphasis on proteome quantification and the understanding protein dynamics on a global, proteome wide scale and of developing relevant methods in intact animals and complex systems. I am the ‘reporting PI’ for the CoPY project. I am Chair of BBSRC Bioscience Skills and Careers Strategy Panel and member of Council of the Biochemical Society. From April 2012 to March 2016 I have a 50% role as Royal Society Industrial Fellow, working with Waters on approaches to handling the dimensional complexity of the proteome."

Institutional positions:

• 1997-1993: Lecturer, Senior Lecturer, Reader, University of Liverpool

• 1993-1999: Chair of Biochemistry, UMIST, Manchester

• 1999-present: Chair of Proteomics, University of Liverpool

• Joint Head, Centre for Proteome Research

• Royal Society Industrial Fellow (from April, 2012)

• Head of Technology Directorate, Faculty of Health and Life Sciences

• Chair of BBSRC Bioscience and Skills Strategy Panel

• Member of Executive and Chair, Education Committee, Biochemical Society

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Professor Claire Eyers BSc PhD

"My main interests lie in the development and application of biochemical and biophysical (mass spectrometry, ion mobility) techniques to study cellular signalling (proteins and their modifications) both qualitatively and quantitatively. While much of the work in my group is the application of methods to investigate specific systems of interest (NF-kB signalling, glycan profiling, response to stress in yeast and mammalian systems), these applied studies are underpinned by fundamental investigations into the behaviour and manipulation of (modified) peptides in the gas-phase to better derive useful information.

My PhD under the supervision of Prof. Sir Philip Cohen in the MRC Protein Phosphorylation Unit at the University of Dundee primed an interest in phosphorylation-regulated signalling, which has underpinned the rest of my research career. I relocated to the University of Colorado, Boulder, where I worked with Prof. Natalie Ahn (HHMI) to develop skills in the MS analysis of phosphopeptides. During this time I was awarded an independent fellowship by the American Heart Association (AHA) and received an AHA postdoctoral prize.

I moved back to the UK in 2004 to work with Professor Simon Gaskell in the Michael Barber Centre at the University of Manchester, a world-renowned expert in biological mass spectrometry, and was subsequently awarded a Royal Society Dorothy Hodgkin Research Fellowship (2007-2011). Having acted as Director for the Michael Barber Centre for Mass Spectrometry from 2009 to 2013, I took up the post of Reader in Proteomics in PFG in May 2013."

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Philip Brownridge BSc PhD

Postdoctoral Researcher

"I started my scientific training as an undergraduate at UMIST reading biochemistry. Towards the end of my degree I was attracted by bioinformatics so I enrolled in the UMIST MSc Computation course and completed a summer research project which used text mining to investigate gene promoter sequences. Towards the end of this project I was offered a PhD opportunity in the Michael Barber Centre for Mass Spectrometry under the supervision of Prof S. Hubbard and Prof. S. Gaskell. This PhD project was split between lab biology and bioinformatics and served as my introduction to proteomics. The main goal of the project was to use chemical crosslinkers to study protein-protein interactions. This project focused on the characterization of modified proteins and peptides by mass spectrometry and on the software to identify modifications. The project produced software that could identify crosslinked species and produced proof of principle data by mapping the subunit interface of some homodimeric test proteins.

My first postdoctoral position within the Protein Function Group (PFG) at the University of Liverpool and was a project aimed to investigate the role of protein isoforms in the relaxation rate of fast twitch muscle fibres. This project involved characterization of the differences between the isoforms, followed by the quantification of the abundance and turnover of the isoforms. 

My second post within the PFG was part of a two centre project to provide absolute quantification data for the yeast proteome. This project is based on QconCAT technology, which is a mass spectrometry based protein quantification strategy, developed by the PFG, and targeted mass spectrometry and between the two sites has produced quantification values for over a thousand yeast proteins. I have now settled into a role maintaining the performance of the PFG in terms of instrument performance, training of personnel and ensuring that our protocols follow the latest techniques and methods.

My research history three projects have given me a wide knowledge of proteomics from classical protein chemistry through to cutting edge mass spectrometry. The protein crosslinking project required knowledge of protein chemistry and employed protein and peptide derivatisation, MS techniques to detect low abundance modified peptides against a complex background including LC-MS/MS. Characterisation of the protein isoforms required two-dimensional electrophoresis, determination of turnover was performed by dynamic SILAC and quantification of the isoforms, the use of targeted mass spectrometry.

The yeast protein quantification project required high throughput targeted mass spectrometry and has allowed me to become an expert in label and label free quantification of proteins. I have analytical and maintenance experience on a wide variety of proteomic equipment including mass spectrometers: MALDI-ToF (Bruker UltraFlex), triple quadrupole mass spectrometers for targeted analysis (Waters Xevo TQ and TQS) and the high resolution mass spectrometers necessary for modern proteomic analysis (Thermo Scientific Orbitrap Velos and QExactive, Waters Synapt G2); and also the accompanying nanoflow LC equipment (Waters NanoAquity and Thermo Scientific 3000 RSLC)."

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For more information access the Centre for Proteome Research's website