Professor of Biophysics

Our research

In the last 15 years our research has been focused on the development of methods of characterising the structure, dynamics and interactions of proteins in previously inaccessible states. These methods are based on the use of experimental data, in particular from nuclear magnetic resonance spectroscopy, as structural restraints in molecular dynamics simulations. Through this approach it is possible to obtain 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 generating aggregate species that are associated with neurodegenerative disorders such as Alzheimer's and Parkinson's diseases.

Application to neurodegenerative diseases

More recently, these studies have led us to investigate 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, we are developing approaches to prevent or delay misfolding disorders based on the enhancement of our quality control mechanisms against protein aggregation.

Watch Professor Vendruscolo discuss his research

Take a tour of the Una Finlay Laboratory in the Centre for Misfolding Diseases

Publications

The MUMO (minimal under-restraining minimal over-restraining) method for the determination of native state ensembles of proteins.
B Richter, J Gsponer, P Várnai, X Salvatella, M Vendruscolo
J Biomol NMR
(2007)
37
Growth with memory
M Marsili, M Vendruscolo
Europhysics Letters
(2007)
37
A PDZ domain recapitulates a unifying mechanism for protein folding
S Gianni, CD Geierhaas, N Calosci, P Jemth, GW Vuister, C Travaglini-Allocatelli, M Vendruscolo, M Brunori
Proc Natl Acad Sci U S A
(2007)
104
Hot sandpiles
G Caldarelli, A Maritan, M Vendruscolo
EPL (Europhysics Letters)
(2007)
35
BPPred: a Web-based computational tool for predicting biophysical parameters of proteins.
CD Geierhaas, AA Nickson, K Lindorff-Larsen, J Clarke, M Vendruscolo
Protein Sci
(2006)
16
Geometry, energetics, and dynamics of hydrogen bonds in proteins: structural information derived from NMR scalar couplings.
J Gsponer, H Hopearuoho, A Cavalli, CM Dobson, M Vendruscolo
J Am Chem Soc
(2006)
128
Structural biology. Dynamic visions of enzymatic reactions.
M Vendruscolo, CM Dobson
Science (New York, N.Y.)
(2006)
313
Characterization of the residual structure in the unfolded state of the Δ131Δ fragment of staphylococcal nuclease
CJ Francis, K Lindorff-Larsen, RB Best, M Vendruscolo
Proteins
(2006)
65
Relation between native ensembles and experimental structures of proteins.
RB Best, K Lindorff-Larsen, MA DePristo, M Vendruscolo
Proceedings of the National Academy of Sciences
(2006)
103
A protein evolution model with independent sites that reproduces site-specific amino acid distributions from the Protein Data Bank.
U Bastolla, M Porto, HE Roman, M Vendruscolo
BMC Ecology and Evolution
(2006)
6

Research Interest Groups

Telephone number

01223 763873

Email address