Biography
I am an expert in structural biology, specializing in NMR spectroscopy and in which I integrate structural techniques (NMR, cryoEM) and computational biology (all-atom simulations) to (a) derive high-resolution structural and dynamic information of complex biological systems (b) provide detailed molecular descriptions of dynamic conformational change on different timescales, self-assembly processes and interactions; (c) bridge our understanding of dynamic processes as they occur within the context of the cellular environment. These areas of interest have been developed over a 20-year period, grounded in a foundation of chemistry and structural biology developed during my doctoral and post-doctoral studies in world-leading research groups in the USA and UK. My primary interests relate to understanding the basis of protein folding and misfolding as it occurs during protein biosynthesis on the ribosome, and correlating these processes with the onset of human conformational diseases, including neurodegeneration and respiratory diseases. These interests are driven by the development and application of NMR methodology to study non-traditional targets including high molecular weight sized biological systems such as protein biosynthesis machinery (e.g. ribosome (2.5 MDa)) and protein interactions, self-assembly and aggregation processes, also e.g. amyloid fibrils/antitrypsin polymers (>nm)) and in-cell NMR measurements. Additional features of my research also include developing NMR techniques to enhance (signal) sensitivity to overcome challenges associated with studying unstable biological complexes; and analytical solutions to derive rich protein-ligand interactions information encoded within NMR correlation spectra.