Past Postdoc
Emma Silvester
Mark Hickling
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
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.
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
Publications
CONTACT INFORMATION:
david.dias AT chem.ox.ac.uk
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
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.
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