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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

Protein folding and misfolding: a paradigm of selfassembly and regulation in complex biological systems

M Vendruscolo, J Zurdo, CE MacPhee, CM Dobson

– Philos Trans A Math Phys Eng Sci

(2003)

361,

1205

(doi: 10.1098/rsta.2003.1194)

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,

243

(doi: 10.1007/s00239-002-2350-0)

Protein folding: bringing theory and experiment closer together

M Vendruscolo, E Paci

– Current Opinion in Structural Biology

(2003)

13,

82

(doi: 10.1016/S0959-440X(03)00007-1)

Self-consistent determination of the transition state for protein folding: application to a fibronectin type III domain.

E Paci, J Clarke, A Steward, M Vendruscolo, M Karplus

– Proceedings of the National Academy of Sciences

(2003)

100,

394

(doi: 10.1073/pnas.232704999)

Protein folding using contact maps and contact vectors

M Vendruscolo

– ARTIFICIAL INTELLIGENCE AND HEURISTIC METHODS IN BIOINFORMATICS

(2003)

183,

75

(link to publication)

Validity of Go models: Comparison with a solvent-shielded empirical energy decomposition

E Paci, M Vendruscolo, M Karplus

– Biophys J

(2002)

83,

3032

(doi: 10.1016/s0006-3495(02)75308-3)

Determination of the structures of distinct transition state ensembles for a β-sheet peptide with parallel folding pathways

R Davis, CM Dobson, M Vendruscolo

– Journal of Chemical Physics

(2002)

117,

9510

(doi: 10.1063/1.1516784)

Determination of a Transition State at Atomic Resolution from Protein Engineering Data

E Paci, M Vendruscolo, CM Dobson, M Karplus

– Journal of molecular biology

(2002)

324,

151

(doi: 10.1016/s0022-2836(02)00944-0)

Lack of Self-Averaging in Neutral Evolution of Proteins

U Bastolla, M Porto, HE Roman, M Vendruscolo

– Physical Review Letters

(2002)

89,

208101

(doi: 10.1103/physrevlett.89.208101)

Small-world view of the amino acids that play a key role in protein folding

M Vendruscolo, NV Dokholyan, E Paci, M Karplus

– Physical Review E Statistical Physics Plasmas Fluids and Related Interdisciplinary Topics

(2002)

65,

61910

(doi: 10.1103/PhysRevE.65.061910)