Professor Sir David Klenerman
We are interested in developing and applying a range of new biophysical methods, based on laser fluorescence spectroscopy and scanning probe microscopy, to important problems in biology, which have not been addressed to date due to the lack of suitable tools. By studying molecules one at time, specific complexes in a mixture can be identified and analysed without the need for any separation. With our collaborators we are exploiting single molecule fluorescence spectroscopy to probe the intramolecular dynamics, conformations and function of range of biologically important molecules and processes including the T-cell receptor on live cells and protein folding. In collaboration with Professor Dobson we are also probing the early stages of the oligomerisation of proteins involved in many neurodegenerative diseases.
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Ubiquitin chain conformation regulates recognition and activity of interacting proteins. Nature 492, 266-270 (2012). Direct Observation of the Interconversion of Normal and Toxic Forms of alpha-Synuclein. Cell 149, 1048-1059 (2012). The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-beta(1-40) peptide. Nature structural & molecular biology 19, 79-83 (2012). Nanoscale live-cell imaging using hopping probe ion conductance microscopy. Nature Methods 6, 279 - 281 (2009) Direct characterization of amyloidogenic oligomers by single-molecule fluorescence. Proc. Natl. Acad. Sci. USA 105, 14424-14429 (2008). Accurate whole human genome sequencing using reversible terminator chemistry. Nature 456, 53-59 (2008).