All cells possess molecular chaperones, the action of which can assist proteins in folding or target them for degradation. The molecular chaperone Hsc70 contributes to protein maturation, translocation and repair, and drives the functional cycle of other proteins, including auxilin and steroid hormone receptors. Interaction of Hsc70 with its substrates depends on a large ATP-dependent conformational change of Hsc70. We have designed fluorescent variants of this chaperone in which the conformational change is reported by changes in the intensity and wavelength of the fluorescence and used these variants to follow the conformation of single Hsc70 molecules. A doctoral student is sought to use this construct to extend this work characterising Hsc70 conformational change at the single molecule level. The successful candidate will have demonstrated an interest in at least one of: protein biochemistry, biophysics, or statistical analysis of single molecule data.