About

We are interested in the structure and function of the contractile apparatus of muscle; the myofibril, the structure and functions of the myosin superfamily, the molecular motors kinesin and dynein, and microtubule associated proteins.

We use a wide range of techniques to investigate the structure and function of the muscle proteins myosin, titin and actin:

• wet biochemistry (protein isolation, expression and characterisation)
• biophysical methods (eg analytical ultracentrifugation, atomic force microscopy)
• light microscopy (confocal, time-lapse fluorescence, deconvolution and super-resolution microscopies)
• developing software to analyse super-resolution images
• electron microscopy, including time-resolved cryo-EM
• molecular genetic tools and cell biology (tissue culture, live cell imaging)

We also investigate cell behaviour, and the dynamic behaviour of molecular motors within cells, using time-lapse phase and fluorescence microscopy, our new instant structured illumination microscope, and dSTORM and PALM.

Our research forms part of the major effort in structural biology at the University of Leeds.