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Dr Megan Wright
Dr J.H. Tomlinson
Prof Michelle Peckham
No more applications being accepted
Competition Funded PhD Project (European/UK Students Only)
About the Project
Proteins form spatially organized, dynamic complexes in cells, giving rise to signaling networks essential for maintaining cellular function. In this project, you will develop new tools for directly labelling proteins in their native cellular environment. Our approach uses Affimers (small antibody alternatives) to direct the transfer of labels from a chemical tool to a target protein. You will design and synthesise tools that exploit different transfer chemistries and labels, and express and purify Affimers that bind target proteins implicated in cancer. This toolset will be used to track proteins via live cell and super-resolution imaging, and to tag proteins and their interacting partners for isolation and analysis by proteomics. You will apply this platform to analyze proteins central to signaling networks that are dysregulated in cancer.
For this interdisciplinary project, you will join an ongoing collaboration of three groups with expertise in chemical biology (Dr Wright), protein engineering (Dr Tomlinson) and super-resolution imaging (Prof. Peckham). This project would ideally suit a candidate with synthetic chemistry skills and a strong interest in applying chemistry to biological problems.
For this interdisciplinary project, you will join an ongoing collaboration of three groups with expertise in chemical biology (Dr Wright), protein engineering (Dr Tomlinson) and super-resolution imaging (Prof. Peckham). This project would ideally suit a candidate with synthetic chemistry skills and a strong interest in applying chemistry to biological problems.
Funding Notes
White Rose BBSRC Doctoral Training Partnership in Mechanistic Biology
4 year fully-funded programme of integrated research and skills training, starting Oct 2019:
• Research Council Stipend
• UK/EU Tuition Fees
• Conference allowance
• Research Costs
Requirements:
At least a 2:1 honours degree or equivalent. We welcome students with backgrounds in biological, chemical or physical sciences, or mathematical backgrounds with an interest in biological questions.
EU candidates require 3 years of UK residency in order to receive full studentship
Not all projects advertised will be funded; the DTP will appoint a limited number of candidates via a competitive process.
https://biologicalsciences.leeds.ac.uk/directory/research-opportunities
4 year fully-funded programme of integrated research and skills training, starting Oct 2019:
• Research Council Stipend
• UK/EU Tuition Fees
• Conference allowance
• Research Costs
Requirements:
At least a 2:1 honours degree or equivalent. We welcome students with backgrounds in biological, chemical or physical sciences, or mathematical backgrounds with an interest in biological questions.
EU candidates require 3 years of UK residency in order to receive full studentship
Not all projects advertised will be funded; the DTP will appoint a limited number of candidates via a competitive process.
https://biologicalsciences.leeds.ac.uk/directory/research-opportunities
How good is research at University of Leeds in Biological Sciences?
Research output data provided by the Research Excellence Framework (REF)
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Career overview
Dr Megan Wright obtained a PhD in Chemical Biology from Imperial College London in 2013, where she worked under the supervision of Prof. Edward Tate on the development of chemical tools to study protein lipidation in protozoan parasites. Following her PhD, she was awarded an EPSRC Doctoral Prize Fellowship, allowing her to remain at Imperial for an additional year. Dr Wright then received a Marie Curie Fellowship to conduct postdoctoral research at the Technical University of Munich, Germany, hosted by Prof. Stephan Sieber. In 2016, she joined the University of Leeds as a University Academic Fellow, a tenure-track position equivalent to Lecturer, and was promoted to Associate Professor in 2022. Her research group focuses on the development of chemical tools to study biological mechanisms.
Research interests
Dr Wright''s research employs the creativity of chemistry to understand fundamental biology and address significant questions in health and disease. Her work focuses on chemical proteomics, developing chemical tools to detect and manipulate small molecule-protein interactions, which include the modification of proteins with small molecules, drug binding to enzymes, and signal-receptor interactions. This research is highly interdisciplinary, encompassing organic and peptide synthesis, protein biochemistry, cell biology, and quantitative mass spectrometry-based proteomics. Dr Wright is particularly interested in exploring molecular interactions within living systems. Her research examines the interplay between bacterial pathogens and host cells, investigating how cells communicate and manipulate each other using small molecule signals. A key area of her work involves ''weaponising'' compounds with photo- or chemically-reactive functionalities to stabilise their interactions with protein targets. To facilitate studies in live cells, she develops probes equipped with small, minimally disruptive tags that serve as handles for selective labelling of probe-protein complexes for analysis. Current projects in Dr Wright''s group include developing new chemical tools to understand communication between human and bacterial cells, understanding protein-protein interactions through chemical tools and mass spectrometry, discovering new anti-infectives and elucidating their modes of action, and designing chemical tools to map redox changes to proteins in cells.
Chemical Biology
Proteomics
Organic Synthesis
Biochemistry
Chemical Tools
Protein Lipidation
Small Molecule-Protein Interactions
Drug Binding
Signal-Receptor Interaction
Interdisciplinary Research
Mass Spectrometry
Cell Biology
Redox Changes
Anti-Infectives
Protein-Protein Interactions
Bacterial Pathogens
Host-Cell Communication
Chemical Probes
Selective Labelling.
Career overview
Dr Jennifer Tomlinson obtained her PhD at the University of Sheffield in 2009, where she conducted NMR studies on the effects of pH on protein structure under the supervision of Prof. Mike Williamson. Following her PhD, she undertook a postdoctoral Wellcome Trust VIP fellowship at the University of Sheffield from 2009 to 2010, focusing on NMR studies of intrinsically disordered peptides. Dr Tomlinson then joined the University of Leeds as a postdoctoral researcher in the lab of Dr Alex O''Neill, where she worked from 2010 to 2017. In 2018, she was awarded the Royal Society Dorothy Hodgkin Research Fellowship at the University of Leeds. Her research primarily centres on structural biology, utilising NMR spectroscopy and biophysical techniques to investigate protein structure and dynamics, particularly in relation to antibiotic resistance mechanisms.
Research interests
Dr Tomlinson''s research focuses on structural biology, employing techniques such as NMR spectroscopy and other biophysical methods to investigate protein structure and dynamics. She aims to understand the molecular mechanisms underlying resistance to clinically significant antibiotics, particularly those that involve allosteric effects and protein dynamics. Dr Tomlinson highlights the critical public health issue of antibiotic resistance, which poses a significant threat to effective bacterial infection treatment. Her work includes studying the mechanism of resistance to fusidic acid, which inhibits bacterial protein synthesis by binding to Elongation Factor G (EF-G). She investigates how the protein FusB mediates resistance by altering the dynamics of EF-G in stalled complexes, contributing to a deeper understanding of antibiotic resistance mechanisms.
NMR Spectroscopy
Structural Biology
Antibiotic Resistance Mechanisms
Protein-Protein Interactions
Protein Dynamics
Biophysical Techniques
Molecular Mechanisms
Allosteric Effects
Bacterial Infections
Public Health Crisis
Fusidic Acid
Elongation Factor G
Antibiotic Resistance
Protein Synthesis
Intrinsically Disordered Peptides
Research Fellowship
Postdoctoral Research
PhD Studies
Protein Structure
Stability
Dynamics
Infectious Diseases.
Career overview
Professor Michelle Peckham graduated in Biology (Physiology of Organisms) from the University of York in 1981 and completed a PhD with Professor Roger Woledge in the Physiology Department at University College London, focusing on the energetics of muscle contraction, which she was awarded in 1984. Following her PhD, she briefly worked with Professor Woledge before moving to the Biophysics Department at King''s College London, where she collaborated with Professor Malcolm Irving from 1985 to 1987 to demonstrate the use of birefringence as a reporter of myosin cross bridge orientation in skeletal muscle. She then worked at the University of California, San Francisco, from 1987 to 1988, before returning to the Biology Department at the University of York to work with Professors David White and John Sparrow on insect flight muscle kinetics from 1988 to 1990. During this time, she engineered mutations in contractile proteins into flight muscle actin and employed advanced biophysical measurements to assess their effects on contraction, resulting in a publication in Nature in 1990. In 1990, she was awarded a Royal Society University Research Fellowship and moved to the Biophysics Department at King''s College London, where she established her own laboratory and began using molecular biology and cell culture techniques to study the cytoskeleton in cultured muscle cells. In 1997, she joined the University of Leeds as a Lecturer, progressing through the ranks to Senior Lecturer, Reader, and ultimately Professor in 2010. Her research interests expanded to include imaging and confocal microscopy, particularly developing super-resolution techniques at Leeds over the past 5 to 10 years, including the creation of Affimers for STORM imaging. Her work has also encompassed structural biology, notably the discovery and characterisation of single alpha helices in proteins, and her laboratory recently solved the structure of the shutdown state of myosin using Cryo-EM. Professor Peckham has trained over 40 postgraduate and postdoctoral researchers and served as the president of the Royal Microscopical Society from 2016 to 2019. She is currently the Executive Honorary Secretary of the RMS and a Wellcome Trust Investigator, focusing on the regulation of motor protein activity.
Research interests
Professor Peckham''s research focuses on the cytoskeleton, specifically investigating how myosins and other motor proteins function within cells and how mutations in cytoskeletal proteins can lead to disease. The laboratory employs a variety of techniques, including Cryo-electron microscopy (Cryo-EM), confocal microscopy, super-resolution imaging, and biochemical and biophysical methods to explore these areas. Significant contributions include solving the structure of the shutdown state of smooth muscle myosin, which was published in Nature in December 2020, revealing insights into how myosin transitions to this state and the role of phosphorylation in its activation. The laboratory has developed advanced imaging systems, such as a 3D PALM/STORM system and an instant structured illumination microscope (iSIM), enhancing the ability to conduct live cell imaging and achieve resolutions significantly better than conventional methods. Professor Peckham''s work also extends to collaborations aimed at developing small non-antibody binding proteins known as Affimers for improved super-resolution imaging of cytoskeletal proteins. Recent studies have utilised stimulated emission depletion (STED) microscopy to investigate structural changes in Z-discs in diseased hearts, with findings published in Frontiers in Cardiovascular Medicine in 2023. Research interests encompass the roles of myosins in diseases, including cancer, where specific myosins are found to be overexpressed in prostate cancer, and the differentiation of muscle cells in culture, focusing on the organisation of the cytoskeleton. Current PhD projects in the lab include the use of artificial intelligence to analyse super-resolution microscopy images, the development of Affimers for visualising myosins, and the impact of heart muscle diseases on protein organisation. Overall, Professor Peckham''s research integrates structural biology, advanced imaging techniques, and molecular biology to further understand the cytoskeleton''s role in health and disease.
Cytoskeleton
Myosin
Actin
Molecular Motors
Super-Resolution Imaging
Electron Microscopy
Biochemical Techniques
Muscle Contraction
Imaging Techniques
Structural Biology
Cryo-EM
Affimers
Disease Mechanisms
Cancer
Muscle Cell Differentiation
Biophysical Measurements
Confocal Microscopy
Protein Structure
Sarcomeric Proteins
Heart Disease
AI in Microscopy
Drosophila Melanogaster
Insect Flight Muscle
Contractile Proteins
Regulatory Light Chain
Z-Discs
Dilated Cardiomyopathy.
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