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

Energetics of enzyme stability.
M Vendruscolo
Trends Biotechnol
(2002)
20
Assessment of the Quality of Energy Functions for Protein Folding by Using a Criterion Derived With the Help of the Noisy Go Model
M Vendruscolo
Journal of biological physics
(2001)
27
Connectivity of neutral networks and structural conservation in protein evolution
U Bastolla, M Porto, HE Roman, M Vendruscolo
J. Mol. Evol.
(2001)
56
Generalized comparative modeling (GENECOMP): a combination of sequence comparison, threading, and lattice modeling for protein structure prediction and refinement.
A Kolinski, MR Betancourt, D Kihara, P Rotkiewicz, J Skolnick
Proteins Structure Function and Bioinformatics
(2001)
44
How to guarantee optimal stability for most representative structures in the protein data bank
U Bastolla, J Farwer, EW Knapp, M Vendruscolo
Proteins Structure Function and Bioinformatics
(2001)
44
Three key residues form a critical contact network in a protein folding transition state.
M Vendruscolo, E Paci, CM Dobson, M Karplus
Nature
(2001)
409
Comparison of two optimization methods to derive energy parameters for protein folding: Perceptron and Z score
M Vendruscolo, LA Mirny, EI Shakhnovich, E Domany
Proteins: Structure, Function, and Genetics
(2000)
41
Toward an energy function for the contact map representation of proteins.
K Park, M Vendruscolo, E Domany
Proteins Structure Function and Genetics
(2000)
40
Structurally constrained protein evolution: Results from a lattice simulation
U Bastolla, M Vendruscolo, HE Roman
European Physical Journal B
(2000)
15
A statistical mechanical method to optimize energy functions for protein folding.
U Bastolla, M Vendruscolo, EW Knapp
Proceedings of the National Academy of Sciences of the United States of America
(2000)
97

Research Interest Groups

Telephone number

01223 763873

Email address