Soft Matter & Biophysical Chemistry Award 2013 Winner
University of Cambridge
For his pioneering work integrating experimental data with computer simulations, transforming our understanding of the nature and interactions of proteins.
About the Winner
Professor Michele Vendruscolo received a doctorate degree in Condensed Matter Physics in 1996 from the International School for Advanced Studies in Trieste (Italy). He then spent two years as post-doctoral fellow at the Weizmann Institute of Science (Israel) where he worked with Eytan Domany on computational methods to study the protein folding problem.
In 1999 he moved to the University of Oxford as an EMBO post-doctoral fellow, where in collaboration with Chris Dobson and Martin Karplus he developed a strategy to incorporate experimental information to generate structural restraints in molecular simulations of proteins. In 2001 he joined the Department of Chemistry at the University of Cambridge as a Royal Society University Research Fellow, becoming a Lecturer in 2006, a Reader in 2008 and a Professor in 2010.
He has developed a series of methods to characterise the structure and dynamics of proteins in previously inaccessible states. These methods are based on the use of experimental data, in particular from Nuclear Magnetic Resonance Spectroscopy, as restraints in molecular dynamics simulations.
Through this approach he has obtained information about a variety of protein conformations, as for example those populated during the folding process, and about protein interactions in complex environments, including those relating to the toxic aggregation-prone species that are the molecular origin of misfolding disorders such as Alzheimer's disease and type II diabetes.
His research interests are also increasingly focused on the investigation of the physico-chemical principles of proteins homeostasis and their application to the development of therapeutic strategies against neurodegenerative diseases. Starting from the observation that proteins are expressed in the cell at levels close to their solubility limits, he is investigating approaches to prevent or delay misfolding disorders based on the enhancement of our quality control mechanisms against protein aggregation.