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Dr Aneika Leney
Prof H J Cooper
No more applications being accepted
Funded PhD Project (European/UK Students Only)
About the Project
Microalgae are becoming of increasing economic interest due to their application as a natural source of compounds such as lipids, pigments, proteins and polysaccharides. Of these, natural pigments such as phycobiliproteins, are of particular interest due to their biotechnological applications in food colourants, pharmaceuticals, and the cosmetic industry. One example of a phycobiliprotein being phycocyanin, the most commonly used natural blue pigment in the food industry for products such as jelly and bubble gum. Phycobiliproteins vary in colour and are the most fluorescent molecules known to date. Moreover, they are 20 times more fluorescent than any organic dye we are capable of synthesizing. Many phycobiliproteins are known to exist, however, few are being utilized to their full potential. This is mainly due to the lack of knowledge on the proteins overall composition, hindering greatly their wide spread applications.
The project will aim to characterise phycobiliproteins from red algae and develop ways to utilize these powerful systems in biotechnological applications. The project will involve the use of native mass spectrometry to analyse these large protein complexes. Throughout the PhD, you will gain hands on training in state-of-the-art mass spectrometry techniques associated with the analysis of proteins and protein complexes. In addition, you will use UV absorbance, SDS PAGE and alternative biochemical techniques. Thus after completion of the PhD, many career paths will be possible.
Birmingham has an excellent reputation in mass spectrometry research. Ideal applicants will have a strong background in biochemistry. Applicants do not need experience in mass spectrometry but should be quick learners and enthusiastic to learn mass spectrometry-based techniques.
The project will aim to characterise phycobiliproteins from red algae and develop ways to utilize these powerful systems in biotechnological applications. The project will involve the use of native mass spectrometry to analyse these large protein complexes. Throughout the PhD, you will gain hands on training in state-of-the-art mass spectrometry techniques associated with the analysis of proteins and protein complexes. In addition, you will use UV absorbance, SDS PAGE and alternative biochemical techniques. Thus after completion of the PhD, many career paths will be possible.
Birmingham has an excellent reputation in mass spectrometry research. Ideal applicants will have a strong background in biochemistry. Applicants do not need experience in mass spectrometry but should be quick learners and enthusiastic to learn mass spectrometry-based techniques.
Funding Notes
We encourage applications all year round. Birmingham has a thriving international PhD community. Applicants should indicate how they intend to fund their studies. Candidates who have successfully gained competitive funding from outside the UK are encouraged to apply.
For further information on applying for a MIBTP studentship please visit: https://www.birmingham.ac.uk/research/activity/mibtp/index.aspx
For further information, please refer to the School of Biosciences website. https://www.birmingham.ac.uk/schools/biosciences/courses/postgraduate/phd/index.aspx.
http://leney-masss-spectrometry.com
For further information on applying for a MIBTP studentship please visit: https://www.birmingham.ac.uk/research/activity/mibtp/index.aspx
For further information, please refer to the School of Biosciences website. https://www.birmingham.ac.uk/schools/biosciences/courses/postgraduate/phd/index.aspx.
http://leney-masss-spectrometry.com
References
Relevant Publications:
Leney A.C.*, Tschanz A., Heck A.J.R. Connecting color with assembly in the fluorescent B-phycoerythrin protein complex. FEBS J. (2018) 285(1): 178-187.
Leney A.C., Heck A.J.R. Native mass spectrometry: what is in the name? J. Am. Soc. Mass Spectrom. (2017) 28(1): 5-13.
Leney A.C.*, Tschanz A., Heck A.J.R. Connecting color with assembly in the fluorescent B-phycoerythrin protein complex. FEBS J. (2018) 285(1): 178-187.
Leney A.C., Heck A.J.R. Native mass spectrometry: what is in the name? J. Am. Soc. Mass Spectrom. (2017) 28(1): 5-13.
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Career overview
Dr Aneika Leney graduated from the University of York in 2008 with a BSc in Biochemistry, during which she undertook an industrial placement at GlaxoSmithKline that sparked her interest in Mass Spectrometry. She completed her PhD in 2013 at the University of Leeds, where she was supervised by Professors Sheena Radford and Alison Ashcroft at the Astbury Centre, focusing on using mass spectrometry to study protein structure and function. Following her PhD, Dr Leney moved to Canada to join the Alberta Glycomics Centre, where her post-doctoral research involved developing novel methodologies to monitor protein-ligand interactions. She then worked at a leading laboratory at Utrecht University in the Netherlands, conducting significant proteomics research under the supervision of Professor Albert Heck, concentrating on protein post-translational modifications and their effects on protein function. Currently, at the University of Birmingham, Dr Leney leads her own research group that employs advanced mass spectrometry techniques to analyse proteins and protein complexes, addressing biological questions related to protein communication and functionality. Her research also investigates the potential biotechnological applications of protein modifications, including uses in food colouring, protein visualisation, and solar energy harvesting.
Research interests
Dr Leney''s research focuses on structural biology-based mass spectrometry, specifically on protein post-translational modifications and their role in communication or miscommunication in diseases. She is exploring how protein modifications can be utilised for biotechnological applications, including food colouring, protein visualisation, and harvesting light energy for solar panels. Dr Leney leads a research group that employs state-of-the-art mass spectrometry techniques to analyse proteins and protein complexes, aiming to understand how proteins communicate and switch between active and inactive states. Her research also involves developing novel techniques to analyse protein post-translational modifications and applying these techniques to solve complex biological problems.
Structural Biology
Mass Spectrometry
Protein Post-Translational Modifications
Protein-Ligand Interactions
Protein Structure
Protein Function
Biotechnology Applications
Protein Complexes
Health and Disease
Biochemical Projects
Proteomics Research
Novel Methodology
Biological Communication
Solar Energy Harvesting
Food Colouring
Protein Visualisation
Career overview
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 a 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 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. She has published extensively in peer-reviewed journals and serves on a number of national and international committees, including the Editorial Board for the Journal of the American Society for Mass Spectrometry and the British Mass Spectrometry Society.
Research interests
Professor Helen J. Cooper''s research focuses on the gas-phase ion chemistry of peptides and proteins, with a particular expertise in electron capture dissociation mass spectrometry. She has established the University of Birmingham as a centre of excellence in mass spectrometry research. Her current research includes the development and application of advanced mass spectrometry techniques for the analysis of biomolecular and chemical structures. Key areas of focus include the development of methods for proteomics, understanding the fundamentals of peptide fragmentation, analysis of post-translational modifications, and the integration of ion mobility spectrometry with mass spectrometry. Additionally, she is involved in developing mass spectrometry-based methods for diagnosing inherited disorders in newborns in collaboration with Birmingham Children’s Hospital. Professor Cooper has published extensively in peer-reviewed journals and serves on various national and international committees, including the Editorial Board for the Journal of the American Society for Mass Spectrometry and the British Mass Spectrometry Society.
Mass Spectrometry
Gas-Phase Ion Chemistry
Peptides
Proteins
Electron Capture Dissociation
Proteomics
Peptide Fragmentation
Post-Translational Modifications
Ion Mobility Spectrometry
Biomedical Research
High Performance Mass Spectrometry
Structural Elucidation
Analytical Chemistry
Native Mass Spectrometry Imaging
Liquid Chromatography
Collision Induced Dissociation
Electron Transfer Dissociation
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