Past Postdoc

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

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