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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

Theoretical approaches to protein aggregation

J Gsponer, M Vendruscolo

– Protein and 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 CI2.

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

– Proceedings of the National Academy of Sciences

(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

– J Mol Biol

(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)

Determination of the folding transition states of barnase by using ΦI-value-restrained simulations validated by double mutant ΦIJ-values

X Salvatella, CM Dobson, AR Fersht, M Vendruscolo

– Proceedings of the National Academy of Sciences

(2005)

102,

12389

(doi: 10.1073/pnas.0408226102)

Interpreting dynamically-averaged scalar couplings in proteins.

K Lindorff-Larsen, RB Best, M Vendruscolo

– Journal of Biomolecular NMR

(2005)

32,

273

(doi: 10.1007/s10858-005-8873-0)

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)