Andrew Baldwin


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Andrew studied Natural Sciences at the University of Cambridge, as a member of Trinity College. He completed his PhD in the laboratory of Chris Dobson in the department of Chemistry, studying the biophysical properties of amyloid fibrils. He then moved to Toronto to develop novel NMR techniques for studying protein dynamics under Prof Lewis Kay, with EMBO and CIHR postdoctoral fellowships. This work was subsequently recognised by a presentation of a Harrison-Meldola medal in 2013. Since September 2012, Andrew has been part of Oxford Chemistry as both a BBSRC David Phillip’s fellow and a Fitzjames fellow of Merton College. He is now Professor in Physical and Theoretical Chemistry, and a fellow of Pembroke College. He was awarded the 2016 BRSG-NMRDG NMR prize for ‘excellence in magnetic resonance’ as well as an ERC grant in 2021.

Andrew is a keen martial artist, qualifying as a 5th degree Taekwondo master in 2020.



CONTACT INFORMATION:
andrew.baldwin AT chem.ox.ac.uk
Biochemistry building
South Parks Road, Oxford OX1 3QU


Sonia Khemaissa


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Sonia is a postdoc working on liquid-liquid phase separation properties of some proteins. This particular property leads to the formation of membraneless organelles inside cells, with functions that are not yet fully understood. The aim of her research project is to decipher the function of these liquid droplets as catalysts for chemical reactions. Moreover, she is interested in studying how these proteins could or not interact with each other.
Sonia completed her PhD in 2023 under the supervision of Dr. Sandrine Sagan and Dr. Astrid Walrant at the Laboratoire des Biomolécules at Sorbonne Université in Paris, where she focused on understanding the mechanisms of membrane interaction and cellular uptake of cell penetrating peptides. She also obtained the French aggregation in physics and chemistry in 2019. She likes to spend her free time walking, reading, or meditating.

Virginia Casablancas Antras

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Virginia is a doctoral student with the Systems Approaches to Biomedical Science CDT, and is jointly supervised by collaborators at EliLilly. The main aim of her research is understanding the mechanisms of amyloid protein aggregation and inhibition using NMR and chemical kinetics approaches. She has also recently started working on the partitioning of small molecules into membraneless organelles. She is generally interested in studying biologically relevant phenomena at the protein interaction level, and in the combination of modelling and experimental approaches.  
Virginia’s background is in Biomedical Sciences (UAB, Spain, 2014) and she later completed an MRes in Molecular Biophysics at King’s College London, funded by a LaCaixa Fellowship for Postgraduate Studies in Europe. During her masters thesis in Prof. James McDonnell’s lab, she focused on the structural asymmetry and allostery of the immunoglobulin E constant region. After finishing her Dphil in group she is now working as a postdoc on the project about membraneless organelles.
Outside the lab, Virginia plays the cello in the Oxford Millenium Orchestra, as well as being part of the Oxford University Table Tennis Team.

James Eaton

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My research looks at the nuclear spin physics involved in NMR, focussing on how molecular dynamics can bring NMR magnetisation back to equilibrium (NMR relaxation). When studying large proteins using NMR, the resolution in their spectra is poor due to fast NMR relaxation. NMR is a fantastic technique for studying the dynamics of molecules in solution, but it is difficult to study the dynamics of larger proteins using NMR due to the poor resolution. By looking at the mathematical theory surrounding relaxation, we hope to develop new techniques to increase the resolution of these spectra, enabling larger proteins and complexes to be studied more routinely.

In addition to the project above, I am aiming to perform protein expression and purification of biologically important proteins, particularly those important to protein folding or aggregation. These will then be analysed by NMR to determine their structures and dynamics.

Outside of research, I like to go hiking or to the gym as it helps clear my mind. I can also be often found at one of the many pubs or bars that Oxford has to choose from.

Ben Naylor

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In his part II research project Ben investigated the properties of phase separated protein droplets, and used NMR techniques to do this. Outside of the research, he plays for Oxford Universities Quadball Club. We are happy that Ben decided to stay on for his Dphil!

Morgan Wright

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Morgan is a DPhil working on identifying binding interactions between small molecules and disordered proteins. Disordered proteins play a large role in the onset and proliferation of neurodegenerative disease, yet methods to study these proteins remain elusive. Morgan uses NMR to investigate these systems, aiming to identify small molecules that could one day act as preventative treatments for such diseases.

Past Group Members

Emma Silvester

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Emma completed her PhD in Andrew Turberfield’s Lab in the department of physics, studying the folding properties of DNA and RNA nanostructures. Following her PhD, she worked as a postdoc in the Division of Structural Biology in Kay Grünewald's lab, using DNA nanostructures to develop new tools for cryo-electron microscopy and tomography. In the Baldwin lab, Emma was using cryo-electron tomography to study the structural properties of membraneless organelles, formed by phase separation of intrinsically disordered proteins.

Mark Hickling


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Mark's research is focussed on membraneless organelles and their ability to selectively enrich for certain RNA molecules.  He is investigating how the properties of the RNA and the proteins that constitute these structures affect this poorly understood selection process, and uses a combination of deep sequencing and bioinformatics to do so. Outside of research he is usually found either on the squash court or getting frustrated watching Arsenal play football! 

Charles Buchannan

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Charlie works on biological NMR method development.  He is particularly interested in using NMR to unpick complex disease-relevant questions.  Recently he has developed a technique to extensively characterise pathogen-ligand interactions using Saturation Transfer Difference NMR, underpinned by previous work on NMR spectral deconvolution.  He is now focused on further applying spectral deconvolution to other experiments, aiming to expedite biological work with NMR.  Outside of research, Charlie competed in the Oxford-Cambridge Boat Race in 2019. After completing his PhD he was postdoc in the Baldwin lab for a year and is now postdoc in Marburg.

Gogulan Karunanithy

Gogs completed his undergraduate degree in Chemistry at the University of Oxford, spending his Part II year in the Baldwin Group. He has completed an EPSRC-funded DPhil in the group, and is interested in NMR methodology development. Publications

CONTACT INFORMATION:
gogulan.karunanithy AT keble.ox.ac.uk


Satoshi Kishigami

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Mr. Satoshi Kishigami was a Dphil student at the University of Oxford. His research projects focused on the development of novel chemical probes to investigate structures and dynamics of high molecular weight macromolecules, and mechanistic study for potential treatments against neurodegenerative diseases. His study at Oxford has been founded by Keidanren (Japan Business Federation) Ishizaka Memorial Foundation, Ezoe Memorial Recruit Foundation, Shigeta Foundation and Sakaguchi International Scholarship Foundation.
Satoshi holds BSc in Applied Chemistry from Keio University, Tokyo and he also studied synthetic organic chemistry at Rice University, Texas where he conducted a research project about the synthesis of anti-cancer natural product derivatives under the supervision of Prof K. C. Nicolaou.

David Miguel Dias

David obtained his MSc. in Biochemistry at the University of Coimbra (Portugal). In 2011, he was awarded a PhD fellowship from the Portuguese Foundation for Science and Technology (FCT) to join the Ciulli and Abell laboratories in Cambridge (UK). Here he focused on targetting protein-protein interaction (PPIs) via fragment-based lead discovery approaches. David's work involves a wide set of bophysical methods but he has been mainly using NMR spectroscopy as a tool to screen and structurally validate fragment binding against several targets. David had joined the Baldwin group to explore the relationship between drug discovery and protein dynamics. He is interested in understanding how mechanisms of proteins aggregation in amyloid diseases can be better understood and potentially use that insight as a rationale for hit generation against amyloid-like proteins.

Publications

CONTACT INFORMATION:
david.dias AT chem.ox.ac.uk

Reid Alderson


Reid studied Biochemistry (B.S.) at the University of Wisconsin-Madison, and is now a Ph.D. student in the National Institutes of Health (NIH) Oxford-Cambridge Scholars Program, in which he was also supervised by Ad Bax and Justin Benesch. Alongside other biophysical tools, Reid studied the structure, dynamics, and function of biomolecules with NMR spectroscopy and native mass spectrometry.

Publications

CONTACT INFORMATION:
reid.alderson AT pmb.ox.ac.uk

Magdeline Ira-Nathan

Tim Nott

Tim obtained a PhD in structural biology at the National Institute for Medical Research (NIMR) in the UK, before moving to the Pawson Lab in Toronto, Canada, to pursue a postdoc in cell biology. Here, he studied how living cells are internally compartmentalised, and in particular how phase separation gives rise to liquid droplet-like membraneless organelles and compartments. In the Baldwin Lab, Tim is continuing his research on this theme, focussing on how the internal membraneless organelle environment influences biochemical reactions.
Tim was a Todd-Bird Junior Research Fellow at New College, Oxford.
Tim now runs a group in biochemistry in Oxford, funded by a Henry-Dale Wellcome/RSC fellowship.
Publications

CONTACT INFORMATION:
timothy.nott AT chem.ox.ac.uk

Henrik Müller

Research interests
Fatal neurodegenerative diseases such as Alzheimer’s disease, Parkinson’s disease, and prion diseases (e.g. mad cow disease) share a common cause. Cellular proteins that, under normal circumstances have a functional role in the body, distort and form long amyloid fibrils, which are non-crystalline and heterogeneous, and can even be infectious. Henrik is interested in understanding (i) the structural details of how benign proteins are converted into causative agents of deadly diseases and (ii) the molecular mechanism by which the human defensive system, in the form of chaperoning small heat shock proteins, inhibits the formation of those protein fibrils.


His work involves an inter-disciplinary combination of biophysical techniques such as electron microscopy (EM), atomic force microscopy (AFM), circular dichroism (CD) spectroscopy, differential ultracentrifugation, ion-mobility mass spectrometry (IMS), and chromatographic techniques with cell and animal-based toxicity assays and cutting edge high-molecular weight solution-state and solid-state NMR spectroscopy.

University and college roles and committees
Postdoctoral Research Associate, Department of Chemistry
Junior Research Fellow at Pembroke College
MPLS representative of the Oxford Research Staff Society (OxRSS)

Publications

CONTACT INFORMATION:
henrik.muller AT chem.ox.ac.uk

Mike Barber

Michael completed a biological sciences degree at the University of Leeds and is now enrolled on the interdisciplinary bioscience doctoral training partnership. Michael studies the structure and dynamics of RNA regulatory enzymes and Gaucher's disease associated Glucocerebrosidase.

Mike graduated in September 2016 and now worked in aid and development in Africa.

CONTACT INFORMATION:
michael.barber AT biodtp.ox.ac.uk

Iva Pritišanac

Iva studied Molecular Biology (B.S.) at the University of Zagreb, Croatia, and subsequently moved to the University of Utrecht, the Netherlands, where she graduated in Molecular and Cellular Life Sciences (M.S.). During her master studies Iva focused on structural biology, performing her major and minor research projects in NMR spectroscopy and X-ray crystallography, respectively. Iva's master's thesis focused on the usefulness of distance restraints derived from EPR and sm-FRET spectroscopic techniques as applied to the computational docking of protein-protein and protein-nucleic acid complexes with HADDOCK. Her interest in using restraints from experimental techniques in computational structural biology continues in her PhD research, which focuses on using experimental restraints from solution-state NMR spectroscopy to automate resonance assignment in spectra of high molecular weight proteins.

Iva graduated in December 2016 and now worked in Frankfurt with Prof. Peter Guntert.

Publications

CONTACT INFORMATION:
iva.pritisanac AT magd.ox.ac.uk

Olga Tkachenko

Olga studied Natural Sciences (Biochemistry) at the University of Cambridge as a member of St. Catharine's College, and spent a year as an exchange student at the University of Heidelberg. She is now a DPhil student and a Lamb and Flag Scholar at St John's College. Olga is interested in conformational dynamics of proteins and in combining advanced biophysical methods to study them, and is supervised jointly by Andrew and by Justin Benesch.

Publications

CONTACT INFORMATION:
olga.tkachenko AT sjc.ox.ac.uk