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| Michele Vendruscolo, University of Cambridge |
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| Michele Vendruscolo obtained his PhD in Condensed Matter Physics at SISSA (Trieste, Italy) in 1996. He then spent two years as a postdoctoral researcher at the Deparment of Physics of Complex Systems, under the supervision of Prof. Eytan Domany. In 1999, he moved as an EMBO long-term fellow to the Oxford Centre for Molecular Sciences at the Department of Chemistry of the University of Oxford (UK) to work in collaboration with Prof. Chris Dobson. Since 2001 he is a Royal Society University Research Fellow at the Department of Chemistry of the University of Cambridge (UK).
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Structure determination of native and non-native protein conformations using NMR-derived restraints
Michele Vendruscolo, Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK
In recent years increasingly detailed information about the structures and dynamics of protein molecules has been obtained by innovative applications of NMR techniques and of theoretical methods, in particular molecular dynamics simulations. I will discuss how such approaches can be combined by incorporating a wide range of different types of experimental data as restraints in computer simulations to provide unprecedented detail about the ensembles of structures that describe proteins in a wide variety of states from the native structure to highly unfolded species. This strategy has provided, in particular, new insights into the mechanism by which proteins are able to fold into their native states, or by which they fail to do so and give rise to harmful aggregates that are associated with a wide range of debilitating human diseases.
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