People

Corinne Smith

Professor and Director of WISBIC

Life Sciences

Clathrin-mediated endocytosis, Cryo-electron microscopy, Biophysics

Research

My current research aims to understand the structure and function of large multi-molecular systems, with the remarkable geometric assemblies formed by clathrin at the heart of this. The functions performed by clathrin are important not only for enabling selective uptake of molecules into cells but also because the machinery of endocytosis supports diverse functions vital to the health of an organism, and yet is exploited by pathogens to gain entry into cells.

Receptor-mediated endocytosis allows a cell to choose and absorb the substances it requires. During clathrin-mediated endocytosis a clathrin-coated vesicle is formed which contains only specifically selected cargo. The clathrin coat is central to the ability of the vesicle to choose its contents and requires that clathrin coordinates binding to a large number of adaptor protein partners. There are too many adaptor proteins to be able to bind all at once to clathrin so a process of selection must take place that will determine what is included in the vesicle and control the timing of internalisation. To understand how this works we are using structural biology and biophysics techniques to gain a three dimensional picture of clathrin cages bound to adaptor proteins and to understand the dynamics of coated vesicle assembly and disassembly.

Józef Lewandowski

Professor and Co-Director of WISBIC

Chemistry

Solid-state NMR, Protein dynamics

Research

My research focuses on the development of solid-state NMR methodology and applications of the solution and solid-state NMR to study relationships between structure, dynamics, and activity of biomolecular systems. I am particularly interested in atomic resolution characterization of solid and solid-liquid interface biological systems including, but not limited to, protein complexes, amyloid fibrils, and membrane proteins.

Join us!

We welcome staff, visiting and associate fellows, professional and technical staff, postgraduate and undergraduate students.

Lona Alkhalaf

Assistant Professor

Chemistry

Natural products, Enzymology, X-ray crystallography

Research

Lona Alkhalaf is Assistant Professor in the Department of Chemistry at the University of Warwick, UK. She uses organic chemistry, enzymology and X-ray crystallography to investigate the function, structure and mechanism of enzymatic targets of natural products and of enzymes involved in natural product production, including polyketide synthases, non-ribosomal peptide synthetases, and post assembly line tailoring enzymes.

Jo Collingwood

Professor and Associate Head

Engineering

Metallomics, Neurodegeneration, Metrology

Research

Joanna Collingwood is a Professor and Associate Head of Engineering at the University of Warwick in the UK, where she founded and leads the Trace Metals in Medicine Laboratory. Joanna holds degrees in Physics from York (MPhys) and Warwick (PhD). Her postdoctoral training was at Keele University (UK) and University of Florida (USA), where she held personal research fellowships from the Alzheimer’s Society, the Dunhill Medical Trust, EPSRC, and an Academic Research Fellowship from Research Councils UK. She has a particular interest in the role of iron metabolism in brain disorders, and has contributed to developments in synchrotron spectromicroscopy analysis of metals in human tissues, and in magnetic resonance imaging of iron levels in tissue samples, to inform clinical measurement of iron dysregulation in neurodegenerative disorders. Correlative imaging is increasingly a focus for her laboratory, including methods to enable label free microscopy of organic and inorganic tissue components. Joanna has served on numerous synchrotron facility user groups and panels at UK and European level, on the USA National High Magnetic Field Laboratory User Committee, and has served as Biomagnetics Editor for IEEE Transactions on Magnetics and on the UK STFC and Alzheimer's Society Biomedical Grant Advisory Boards.

Allister Crow

Associate Professor

Life Sciences

Structural Microbiology, Crystallography, CryoEM

Research

The Crow lab use structural and microbiological techniques to understand how bacteria divide, defend themselves from antibiotics and secrete protein toxins.We are especially interested in novel Type VII ABC transporter systems located in the bacterial cell envelope.

Ann Dixon

Reader and Deputy Head of Department

Chemistry

Solution-state NMR, Biological membranes, Membrane proteins

Research

My group is currently focussed in three main research areas, summarised below.

1. Protein biophysics: We use a wide range of complementary biophysical methods (including solution-state NMR spectroscopy) to investigate physical properties of proteins, including structure, interactions, ligand-binding, oligomeric state and stability. Of particular interest are integral membrane proteins (such as immune receptors) and peripheral membrane proteins (e.g. antimicrobial peptides).

2. Protein engineering and design: We have applied methods in protein engineering as well as de-novo protein design to create both soluble and membrane-spanning proteins with predictable and well-defined properties.For example, we have recently designed a small, single-chain variable fragment antibody that retains the activity of the parent Fab, but possess enhanced stability and (when coupled with a tag) improved affinity. We have also designed single-spanning membrane proteins with a range of interaction strengths, to determine how TM sequence defines protein-protein and protein-lipid interactions.This work has potential in the field of synthetic biology.

3. Membrane biophysics: We use a wide range of complementary biophysical and computational methods to investigate the role of lipid composition on properties of the membrane (e.g. membrane curvature, thickness, fluidity, charge etc.) on protein-lipid interactions and downstream biological function.We are also interested in the design, generation and characterisation of model membrane systems with applications in synthetic biology.

Chris Dowson

Professor

Life Sciences

Microbiology, Biochemistry, Drug discovery

Research

Debs Brotherton

Assistant Professor

Life Sciences

Membrane proteins, Cryo-EM, Protein purification

Research

My work centres on expression and purification of membrane proteins to enable structural characterisation of our target proteins: investigating gated ion channels, receptors and secondary transporters, I use techniques that will enhance our understanding of their structure and function. My main goal is to acquire high resolution 3D structures, using either single particle Cryo-EM or X-ray crystallography. We look to capture as many different functional states as we can, by freezing our samples in the presence of substrates and co-factors, to help us understand the dynamics of the proteins’ movements when carrying out their function. We support these structural data with a range of biophysical studies, including transport assays, Mass spectroscopy, binding assays, thermostability assays and microscale isothermal calorimetry. My current work is on Prof. Nick Dale’s Leverhulme grant, continuing to look at carbon dioxide sensitive proteins. The focus of this work is to express gustatory receptors, to allow us to investigate both the structure, and the potential post-translational modification of this family of proteins by carbon dioxide using both Cryo-EM and Mass spectroscopy.

Wing Ying Chow

Assistant Professor

Physics

Solid-state NMR, Extracellular matrix, Collagens, Fungal cell wall

Research

Murray Grant

Elizabeth Creak Chair in Food Security

Life Sciences

Resistosomes, Sialidases, LRR receptors

Research

Matthew Turner

Professor

Physics

Theory, Modelling, Membranes

Research

Séamus Holden

Professor

Life Sciences

Bacterial cell wall, Single molecule FRET, Super-resolution microscopy

Research

My lab studies biophysical principles of bacterial cell wall biosynthesis, with a particular focus on the protein complexes that perform bacterial cell division and elongation. We work primarily with the Gram-positive model organism Bacillus subtilis. Core techniques are in vivo studies of single molecule dynamics in living cells by single molecule tracking and super-resolution microscopy, and in vitro studies of protein structural dynamics by single molecule FRET.

Matthew Jenner

UKRI Future Leaders Fellow & Associate Professor

Chemistry

Mass spectrometry, Crystallography, Biosynthesis

Research

Research in the Jenner Lab focuses on the application of mass spectrometry, in combination with other analytical and structural techniques, to solve complex biological problems. Our primary interest concerns the enzymes involved in natural product biosynthesis.

Jeremy Keown

Assistant Professor

Life Sciences

CryoEM, RNA virus, Viruses

Research

My group studies processes performed by negative sense RNA viruses that infect humans and animals. Each year viruses from these families cause localised epidemics and rare global pandemics. We study members of the influenza virus, hantavirus, nairovirus, and bornavirus families. Much of our research focuses on how these viruses use a virally encoded protein called the polymerase to replicate and transcribe their viral genome.

Our group uses a classical structure/function approach to studying these polymerase, with single particle cryoEM being the structural technique of choice for these large flexible complexes. To identify optimal complexes for cryoEM analysis we use a range of functional assays, biophysical characterisation, and often nanobodies. I have extensive experience in analysing protein, protein-RNA, and protein-protein complexes by cryoEM and X-ray crystallography. In previous projects I have performed cryoET, XChem fragment screening, SAXS, and a regular contributor to CASP.

Sarah Smith

Post-doctoral Research Fellow

Life Sciences

Endocytosis, CryoEM, protein biochemistry

Research

My current research focuses on the biology of clathrin proteins.

Clathrins are self-assembling cytoplasmic proteins that serve to mediate membrane trafficking. At intracellular membranes, individual clathrin subunits surround an invaginating membrane to form a protein coat that assists in cargo capture and vesicle formation.

The process of coated vesicle formation that is facilitated by clathrin proteins is fundamental to a range of cellular processes including: neurotransmission, signal transduction and the regulation of many plasma membrane activities. In short, this process is essential to higher eukaryotic life. Perturbations of clathrin-coated vesicle formation have been linked to numerous pathological conditions including, neurodegeneration, heart disease and tumour formation.

Clathrin cannot recognise membrane or cargo and so an adaptor protein binds the membrane, selects the cargo, and associates with clathrin leading to pit formation. Several adaptor proteins have clathrin binding sites and colocalize with clathrin structures in cells. Our structural knowledge of these adaptor-clathrin interactions and their functional importance, is unclear.

My single particle cryo-electron microscopy work revealed how adaptor protein, AP2 (which recruits clathrin to the plasma membrane), promotes clathrin assembly into a cage-like structure during coat formation by crosslinking different clathrin subunits. This was the first time that a role for AP2 outside of clathrin recruitment had been explored. It also raises the question of whether other adaptor proteins also demonstrate a multi-modal nature of interacting with clathrin.

Using high resolution 3D cryo-electron microscopy and dynamic biophysical techniques, I endeavour to continue to shed light on the interactions that clathrin and its network of binding partners make whilst facilitating coated vesicle formation.

Richard Napier

Professor

Life Sciences

Molecular interaction, Receptor, Transport

Research

Our primary interest is in how the plant hormone auxin works because its actions are the foundations for most of the green plant world. As biochemists, we are fascinated by how specificity is conferred for auxin. Millions of similar, but different small organic molecules cause no reaction at all, whilst the natural hormone molecule (indole-3-acetic acid, IAA) fits into its binding pocket perfectly and in doing so activates the plant world.

We purify members of the auxin receptor family of proteins in the lab and use these in experiments to measure binding using advanced instruments like Biacore SPR (surface plasmon resonance). We are interested in how and why different members of the receptor family show preferences for different auxin mimics and this is important in agriculture because synthetic auxins are vitally important selective herbicides.

Peter O'Connor

Professor

Chemistry

Tandem Mass Spectrometry

Research

Peter B. O'Connor is a leading expert in mass spectrometry, focusing on instrumentation development and applications to complex biochemical problems. His research interests span several key areas:

Fourier Transform Ion Cyclotron Resonance (FTICR) mass spectrometry: O'Connor has made significant contributions to improving FTICR technology, including developing methods for phasing FTICR spectra to enhance resolution and accuracy.

Two-dimensional mass spectrometry (2DMS): He has been instrumental in advancing 2DMS techniques, which allow for comprehensive analysis of complex mixtures without precursor ion isolation. This work led to the establishment of Verdel Instruments Ltd., a spin-out company commercializing 2DMS technology.

Electron Capture Dissociation (ECD): O'Connor's research on ECD mechanisms has significantly improved understanding of peptide and protein fragmentation in mass spectrometry.

Applications in proteomics and structural biology: His work includes detailed structural analysis of proteins, studies on post-translational modifications, and investigations into protein-drug interactions.

Instrumentation development: O'Connor has worked on designing novel mass spectrometers and improving existing technologies, such as developing high-sensitivity preamplifiers for FTICR detection.

Data analysis and informatics: He has contributed to developing advanced algorithms for interpreting complex mass spectra.

O'Connor's research has been well-funded by various sources, including EPSRC, BBSRC, and industrial partners. His work has significant implications for fields such as proteomics, metabolomics, and pharmaceutical research, particularly in areas like drug discovery, disease diagnosis, and understanding protein structure and function.

Peng Wang

Associate Professor

Physics

Cryogenic Electron Microscopy, 3D Imaging, Computational Imaging

Research

My research has been focused primarily on developing novel computational diffractive imaging techniques (ptychography, 4D STEM) for cryogenic electron microscopy (Cryo-EM), liquid EM, light atomic detecting (O, Li elements), low dose imaging (beam sensitive materials), 3D reconstruction and EM field mapping, which can then tackle characterization challenges across the physical and life sciences, ranging from pharmaceutical materials to biological macromolecules.

David Roper

Professor

Life Sciences

Peptidoglycan, Antibiotic-discovery, Anti-microbial resistance

Research

Research in my group is focused on the way in which pathogenic bacteria make their cell walls grow, how that is related to the ways in which they divide and reproduce and also the relationship of these processes to the discovery and resistance to antibiotics.

Phillip Stansfeld

Professor

Life Sciences

Membrane Proteins, Molecular Mechanisms, Computational Biochemistry

Research

David Walker

Principle Technical Specialist

Research Technology Platform

X-ray Diffraction, Structural Solution, Electron Diffraction

Research

I run the X-ray Diffraction facility at Warwick, based in the materials and analytical sciences building, which provides services for structural solution, powder diffraction and SAXS. I am also the Warwick PI for the EPSRC funded National Electron Diffraction Facility and our Electron Diffractometer which allows for structural solution from crystals that are not big enough to be suitable for conventional X-ray crystallography.

Saskia Bakker

Advanced Bioimaging RTP Manager

Research Technology Platform

Cryo-EM, Instrumentation, Sample Preparation

Research

Dr Saskia Bakker manages the Advanced Bioimaging RTP facility. She has a wide knowledge of all the equipment the facility houses, with a special interest in cryo-EM and cryo-tomography, in addition to sample preparation for imaging. Saskia can help users design experiments, or alternatively carry out imaging on behalf of the user.

Alex Cameron

Professor

Life Sciences

X-ray crystallography, membrane proteins, cryo-EM

Research

Claudia Blindauer

Professor

Chemistry

Metalloprotein, zinc, metal homeostasis

Research

We are working in the field of Inorganic Biochemistry, with a focus on structure and dynamics of metal-binding proteins.
This includes studying the coordination chemistry of diamagnetic metal ions such as zinc, copper(I), and cadmium in proteins. We are particularly interested in the molecular mechanisms that govern the movements of zinc within whole organisms (animals, plants, bacteria) and within individual cells.

We use NMR and other spectroscopic techniques to study the structure and reactions of metalloproteins. Other techniques that are indispensable in our work are (native) Electrospray Mass Spectrometry, Elemental Analysis (by ICP-MS) and protein expression and purification.

Chris Corre

Professor

Chemistry and Life Sciences

Natural products, transcriptional regulation, Streptomyces bacteria

Research

Our research group is particularly interested in understanding and exploiting the regulatory mechanisms that control the production of bioactive molecules (e.g. antibiotics, agrochemicals, sunscreen agent) in actinobacteria.

Melissa Webby

Wellcome Career Development Fellow

Life Sciences

Drug resistant pathogens

Bacterial cell mechanism

Cellular imaging

Research

My lab studies how bacteria build and maintain their protective outer shell, known as the cell envelope. This structure is central to antimicrobial resistance, allowing bacteria to adapt to their environment and block harmful molecules. By understanding how the molecular machines that construct the bacterial envelope work together, we aim to identify new antibiotic targets.

We use single-particle cryo-EM to determine the structure of protein complexes critical for envelope maintenance and combine this with protein biochemistry to study their interactions and assembly mechanisms. We also integrate cryo-electron tomography with fluorescence microscopy to visualise where and how these complexes function within the cell, revealing the dynamic architecture of the bacterial envelope.