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

Inhibition of protein crystallization by evolutionary negative design.
JPK Doye, AA Louis, M Vendruscolo
Physical biology
(2004)
1
Comparison of the transition state ensembles for folding of Im7 and Im9 determined using all-atom molecular dynamics simulations with phi value restraints
E Paci, CT Friel, K Lindorff-Larsen, SE Radford, M Karplus, M Vendruscolo
Proteins
(2003)
54
Rare fluctuations of native proteins sampled by equilibrium hydrogen exchange
M Vendruscolo, E Paci, CM Dobson, M Karplus
Journal of the American Chemical Society
(2003)
125
Structures and relative free energies of partially folded states of proteins.
M Vendruscolo, E Paci, M Karplus, CM Dobson
Proceedings of the National Academy of Sciences of the United States of America
(2003)
100
Statistical properties of neutral evolution
U Bastolla, M Porto, HE Roman, M Vendruscolo
Journal of molecular evolution
(2003)
57
Calculation of Mutational Free Energy Changes in Transition States for Protein Folding
K Lindorff-Larsen, E Paci, L Serrano, CM Dobson, M Vendruscolo
Biophysical journal
(2003)
85
Analysis of the distributed computing approach applied to the folding of a small beta peptide.
E Paci, A Cavalli, M Vendruscolo, A Caflisch
Proc Natl Acad Sci U S A
(2003)
100
Protein folding and misfolding: a paradigm of self–assembly and regulation in complex biological systems
M Vendruscolo, J Zurdo, CE MacPhee, CM Dobson
Philosophical Transactions of the Royal Society of London. Series A: Mathematical, Physical and Engineering Sciences
(2003)
361
Connectivity of neutral networks, overdispersion, and structural conservation in protein evolution.
U Bastolla, M Porto, MH Eduardo Roman, MH Vendruscolo
Journal of molecular evolution
(2003)
56
Protein folding: bringing theory and experiment closer together
M Vendruscolo, E Paci
Current opinion in structural biology
(2003)
13

Co-Director

Research Interest Groups

Telephone number

01223 763873

Email address