Professor Godfrey Beddard
University of Edinburgh
Joseph Black Building
David Brewster Road
- Tel: 0131 650 4817
Research has largely focused on developing and then using time-resolved laser methods (on femtosecond and longer time scales) to study a range of phenomena such as radiationless transitions from excited states; rotational diffusion in solutions, membranes and proteins; electron and energy transfer in photosynthetic organisms; electron transfer in organic molecules and in DNA???s, and photo-induced protein folding and unfolding. Protein unfolding under the influence of force has also been extensively studied using Atomic Force Microscopy.
Most recently, a new technique based on the Hadamard transform has been developed for use in time-resolved spectroscopy and most importantly in time-resolved x-ray crystallography.
- The roughness of the protein energy landscape results in anomalous diffusion of the polypeptide backbone. Volk. et al. Phys. Chem. Chem. Phys. (2015), 17, 762-782.
- Time-Resolved Crystallography using the Hadamard Transform. Yorke et al. Nature Methods (2014) ,11, 1131-1134
- Measurement of energy landscape roughness of folded and unfolded proteins Milanesi et al. Proc. Natl. Acad. Sci. (USA). (2012), 109, 19563–19568.
- Mechanically Unfolding the Small, Topologically Simple Protein L Brockwell et al. Biophys. J. (2005), 89, 506-19
- Pulling geometry defines the mechanical resistance of a beta-sheet protein Brockwell et. al. Nature Structural Biology. (2003), 10, 731-737.