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

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 of the United States of America

(2006)

103

10901

(doi: 10.1073/pnas.0511156103)

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 of the United States of America

(2006)

103

10901

(doi: 10.1073/pna.0511156103)

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

43

(doi: 10.1186/1471-2148-6-43)

Structural comparison of the two alternative transition states for folding of TI I27

CD Geierhaas, RB Best, E Paci, M Vendruscolo, J Clarke

Biophysical Journal

(2006)

91

263

(doi: 10.1529/biophysj.105.077057)

Theoretical approaches to protein aggregation

J Gsponer, M Vendruscolo

Protein & Peptide Letters

(2006)

13

287

(doi: 10.2174/092986606775338407)

Structural interpretation of hydrogen exchange protection factors in proteins: Characterization of the native state fluctuations of C12

RB Best, M Vendruscolo

Structure

(2006)

14

97

(doi: 10.1016/j.str.2005.09.012)

Determination of an ensemble of structures representing the intermediate state of the bacterial immunity protein Im7

J Gsponer, H Hopearuoho, SB-M Whittaker, GR Spence, GR Moore, E Paci, SE Radford, M Vendruscolo

Proc Natl Acad Sci U S A

(2005)

103

99

(doi: 10.1073/pnas.0508667102)

Transition state contact orders correlate with protein folding rates

E Paci, K Lindorff-Larsen, CM Dobson, M Karplus, M Vendruscolo

Journal of molecular biology

(2005)

352

495

(doi: 10.1016/j.jmb.2005.06.081)

Effective interactions between chaotropic agents and proteins.

G Salvi, P De Los Rios, M Vendruscolo

Proteins Structure Function and Bioinformatics

(2005)

61

492

(doi: 10.1002/prot.20626)

Form of Growing Strings

D Marenduzzo, TX Hoang, F Seno, M Vendruscolo, A Maritan

Phys Rev Lett

(2005)

95

098103

(doi: 10.1103/physrevlett.95.098103)