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03 - 05 Sept 2017 Cambridge, UK


 Dr Emanuele Paci

 University of Leeds, UK




Most of my research in the past decade has been devoted to advance understanding of properties of macromolecules in biological contexts, by using computer simulations to establish a relation between physical models and experimental measurements. One unique property of biological polymers such as proteins and RNA is their ability to populate a state characterised by a precisely defined conformation, unlike any man-made polymers. Protein folding is one of the major focuses of our recent research, with a particular interest to the relation between folded structure, unfolding pathway and mechanical properties. Our theoretical and computational research in this field has had impact on the way experiments are performed and interpreted, while mechanical response is increasingly recognised as an essential part of many biological processes.

More recently we have turned our interests to the growth of bacterial pili, rational design of symmetric protein complexes such as capsids (with B. Turnbull), analysis of time resolved X-ray spectroscopy data (with A. Pearson), determination of structure and dynamics of macromolecular compounds from cryo-EM (with S. Muench) and hydrogen-exchange mass spectroscopy experiments (with R. Tuma).

Current major projects include:

  • Rational tools for predicting molecular interactions
  • Molecular biomechanics and adhesion 
  • development of computational methods for structural determination from
  • Computational methods for structure determination from sparse data