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

Prediction of "aggregation-prone" and "aggregation-susceptible" regions in proteins associated with neurodegenerative diseases.

AP Pawar, KF Dubay, J Zurdo, F Chiti, M Vendruscolo, CM Dobson

Journal of Molecular Biology

(2005)

350

379

(doi: 10.1016/j.jmb.2005.04.016)

Detection of non-native hydrophobic interactions in the denatured state of lysozyme by molecular dynamics simulations

E Paci, M Vendruscolo

Journal of Physics: Condensed Matter

(2005)

17

S1617

(doi: 10.1088/0953-8984/17/18/017)

A glimpse at the organization of the protein universe.

M Vendruscolo, CM Dobson

Proceedings of the National Academy of Sciences

(2005)

102

5641

(doi: 10.1073/pnas.0500274102)

Looking at structure, stability, and evolution of proteins through the principal eigenvector of contact matrices and hydrophobicity profiles.

U Bastolla, M Porto, HE Roman, M Vendruscolo

Gene

(2005)

347

219

(doi: 10.1016/j.gene.2004.12.015)

Comparison of Sequence-Based and Structure-Based Energy Functions for the Reversible Folding of a Peptide

A Cavalli, M Vendruscolo, E Paci

Biophysical Journal

(2005)

88

3158

(doi: 10.1529/biophysj.104.055335)

Formation of native and non-native interactions in ensembles of denatured ACBP molecules from paramagnetic relaxation enhancement studies

S Kristjansdottir, K Lindorff-Larsen, W Fieber, CM Dobson, M Vendruscolo, FM Poulsen

J Mol Biol

(2005)

347

1053

(doi: 10.1016/j.jmb.2005.01.009)

Simultaneous determination of protein structure and dynamics

K Lindorff-Larsen, RB Best, MA Depristo, CM Dobson, M Vendruscolo

Nature

(2005)

433

128

(doi: 10.1038/nature03199)

Comparison of the different transition states for folding in TI 127

CD Geierhaas, E Paci, M Vendruscolo, J Clarke

BIOPHYSICAL JOURNAL

(2005)

88

216A

Protein folding and the organization of the protein topology universe.

K Lindorff-Larsen, P Røgen, E Paci, M Vendruscolo, CM Dobson

Trends in Biochemical Sciences

(2005)

30

13

(doi: 10.1016/j.tibs.2004.11.008)

Towards complete descriptions of the free-energy landscapes of proteins.

M Vendruscolo, CM Dobson

Philosophical Transactions of the Royal Society A: Mathematical, Physical and Engineering Sciences

(2004)

363

433

(doi: 10.1098/rsta.2004.1501)