Professor Helen Cooper

Supervisor Details

Contact Details

School of Biosciences, University of Birmingham

Scientific Background

Research Interests

Professor Helen J. Cooper is an expert in the gas-phase ion chemistry of peptides and proteins. She is a world-leader in the field of electron capture dissociation mass spectrometry and is responsible for establishing the University of Birmingham as a centre of excellence in mass spectrometry research.

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:

Development of methods for proteomics.
Fundamentals of peptide fragmentation.
Analysis of post-translational modifications.
Ion mobility spectrometry and mass spectrometry.
Direct surface sampling of dried blood spots.

Research Groups

Cooper Lab

Advanced Mass Spectrometry Facility

Supervision Style

In three words or phrases: Data orientated, direct, supportive.

Provision of Training

In the beginning your training will be supervised predominantly by my experienced postdocs/PhD students, leading to more independence later.

Progression Monitoring and Management

I will expect you to take full ownership of your progression but come to me when you need help troubleshooting.

I like to be kept up to date of progress on a weekly basis.

I have high expectations and will push you to your full potential.

Communication

I am known to email my team/PhD students at all hours of the day and night, however I will not expect you to do the same.

The team has a WhatsApp group chat with which we regularly communicate during the week and weekends. Whilst I expect you to keep up with my/ team communications I will expect you to manage your work/life balance.

I am happy to discuss any issues that are impacting your ability to fulfil your potential or my/our expectations.

PhD Students can expect scheduled meetings with me:

In a group meeting

At least once per week

In year 1 of PhD study

At least once per week

In year 2 of PhD study

At least once per week

In year 3 of PhD study

At least once per week

These meetings will be a mixture of face to face or via video chat or telephone, and I have an open door policy but my pattern of being contactable for an instant response is not predictable.

Working Patterns

Certain tasks in my lab need to occur at set times, and students need to be able to commit to a rota/timetable shared with other members of the team.

Notice Period for Feedback

I need at least 2 week’s notice to provide feedback on written work of up to 5000 words.

MIBTP Project Details

Current Projects (2025-26)

Primary supervisor for:

New tools for structural biology: Native ambient mass spectrometry

See the PhD Opportunities section to see if this project is currently open for applications via MIBTP.

Please Note: The main page lists projects via BBSRC Research Theme(s) quoted and then relevant Topic(s).

New tools for structural biology: Native ambient mass spectrometry

Secondary Supervisor(s): Dr Aneika Leney

University of Registration: University of Birmingham

BBSRC Research Themes: Understanding the Rules of Life (Structural Biology)

Project Outline

Native ambient mass spectrometry (NAMS) is an emerging field that enables label-free characterisation of proteins and their complexes directly from their physiological environment. NAMS has the potential to be an enormously powerful tool for structural biology. For example, NAMS has the potential to provide structural information on a protein-drug complex, or a pathological protein aggregate such as found in Alzheimer’s Disease, directly from the tissue itself, providing unprecedented insight into fundamental biological processes. What’s more, NAMS provides this information in a spatially-defined manner. That is, NAMS may be applied for mass spectrometry imaging. The benefits of NAMS can be illustrated by considering a thin tissue section through a drug-treated tumour. In principle, NAMS would inform on drug-target interactions (i.e., is the drug binding to the correct protein?)) and location of drug target interactions (i.e., is the protein-drug complex in the tumour or healthy tissue?).

The Cooper lab is at the forefront of NAMS research and have demonstrated that intact protein complexes can be extracted from tissue sections by two complementary techniques: liquid extraction surface analysis (LESA) [1, 2] and nanospray desorption electrospray ionisation (nano-DESI) [3, 4]. Despite these promising results, the underlying mechanisms of extraction of native proteins remain unclear, as do the optimum sampling and analysis conditions. The aim of the project is to address these questions and to further develop these techniques for NAMS of a range of tissue types. The research will also involve integration of ion mobility spectrometry techniques with the NAMS techniques to further improve performance. Computational tools for data analysis (protein identification and visualisation of mass spectrometry imaging datasets) will be developed.

References

1. Hale, O.J., et al., J. Am. Soc. Mass Spectrom., 2020, 31, 873-879.

2. Griffiths, R.L., et al., Int. J. Mass Spectrom., 2017, 437, 23-29.

3. Hale, O.J., et al., Native Ambient Mass Spectrometry of an Intact Membrane Protein Assembly and Soluble Protein Assemblies Directly from Lens Tissue. 2022: University of Birmingham eData Repository.

4. Sisley, E.K., et al., J. Am. Chem. Soc., 2022, 144, 2120-2128.

Co-supervisor on a project with Professor James McDonald.

Previous Projects (2024-25)

Primary supervisor for:

New tools for structural biology: Native ambient mass spectrometry

Co-supervisor on a project with Dr Aneika Leney.

Previous Projects (2023-24)

Primary supervisor for:

New tools for structural biology: Native ambient mass spectrometry