Andrew Baldwin


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 currently an Associate 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’.

Andrew is a keen martial artist, qualifying as a 4th degree Taekwondo master in 2011.

andrew.baldwin AT
35-05 Physical and Theoretical Chemistry Laboratory
South Parks Road, Oxford OX1 3QZ


Magdeline Ira-Nathan


Simon Hulse


Satoshi Kishigami


Yixuan Hu

Virginia Casablancas Antras


Charles Buchannan

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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 is also supervised by Ad Bax and Justin Benesch. Alongside other biophysical tools, Reid studies the structure, dynamics, and function of biomolecules with NMR spectroscopy and native mass spectrometry.


reid.alderson AT

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 now started an EPSRC-funded DPhil in the group, and is interested in NMR methodology development. Gogs is a member of Keble College.


gogulan.karunanithy AT

David Miguel Dias

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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 has 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


david.dias AT

Alex Haigh

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.

timothy.nott AT

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)


henrik.muller AT

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.

michael.barber AT

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.


iva.pritisanac AT

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.


olga.tkachenko AT

Rachel Lee


Rachel was a Part II student at New College. Her research focuses on using contact angle analysis to study models of membraneless organelles.

rachel.lee AT

Frances Armytage-Green

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Anna Van Der Zalm

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Anna was a part II student with us during the 2014-2015 academic year. Her project focused on the expression and purification of amyloid beta (1-42) and on the characterization of subunit exchange kinetics within alphaB-crystallin.

Adam Marsden

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Adam was a part II student with us in the 2014-2015 academic year. His project focused on the development of software to create structural models of disordered proteins that are consistent with NMR data.

Ben Girling


Ben was a part II student with us in the 2013-2014 academic year. His project focused on characterising alphaB-crystallin by NMR and mass spectrometry.

Current position: medical student

Elodie Limer

Elodie was a part II student with us during the 2013-2014 academic year. Her project focused on the analysis of NMR lineshapes, with applications to protein-ligand interactions.

Current position:
Principal consultant at ecoVeritas