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Yusuf Hamied Department of Chemistry

 

Professor Michele Vendruscolo

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

The Zyggregator method for predicting protein aggregation propensities.
GG Tartaglia, M Vendruscolo
– Chemical Society reviews
(2008)
37,
1395
(doi: 10.1039/b706784b)
Prediction of aggregation-prone regions in structured proteins
GG Tartaglia, AP Pawar, S Campioni, CM Dobson, F Chiti, M Vendruscolo
– J Mol Biol
(2008)
380,
425
(doi: 10.1016/j.jmb.2008.05.013)
A Coupled Equilibrium Shift Mechanism in Calmodulin-Mediated Signal Transduction
J Gsponer, J Christodoulou, A Cavalli, JM Bui, B Richter, CM Dobson, M Vendruscolo
– Structure (London, England : 1993)
(2008)
16,
736
(doi: 10.1016/j.str.2008.02.017)
Calculation of the free energy barriers in the oligomerisation of Ab
M Cheon, G Favrin, I Chang, CM Dobson, M Vendruscolo
– Frontiers in Bioscience-Landmark
(2008)
13,
5614
(doi: 10.2741/3104)
Biological function in a non-native partially folded state of a protein
F Bemporad, J Gsponer, HI Hopearuoho, G Plakoutsi, G Stati, M Stefani, N Taddei, M Vendruscolo, F Chiti
– The EMBO journal
(2008)
27,
1525
(doi: 10.1038/emboj.2008.82)
PHYS 221-Simultaneous determination of protein structure and dynamics
M Vendruscolo
– ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY
(2008)
235,
(link to publication)
Characterisation of transition state structures for protein folding using 'high', 'medium' and 'low' Φ-values
CD Geierhaas, X Salvatella, J Clarke, M Vendruscolo
– Protein engineering, design & selection : PEDS
(2008)
21,
215
(doi: 10.1093/protein/gzm092)
Determination of the transition state ensemble for the folding of ubiquitin from a combination of Phi and Psi analyses.
P Várnai, CM Dobson, M Vendruscolo
– J Mol Biol
(2008)
377,
575
(doi: 10.1016/j.jmb.2008.01.012)
Protein dynamics under light control.
M Vendruscolo
– Nat Chem Biol
(2008)
4,
449
(doi: 10.1038/nchembio0808-449)
Role of intermolecular forces in defining material properties of protein nanofibrils.
TP Knowles, AW Fitzpatrick, S Meehan, HR Mott, M Vendruscolo, CM Dobson, ME Welland
– Science
(2007)
318,
1900
(doi: 10.1126/science.1150057)
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Telephone number

01223 763873

Email address

mv245@cam.ac.uk

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