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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

Blind testing of routine, fully automated determination of protein structures from nmr data
A Rosato, JM Aramini, C Arrowsmith, A Bagaria, D Baker, A Cavalli, JF Doreleijers, A Eletsky, A Giachetti, P Guerry, A Gutmanas, P Güntert, Y He, T Herrmann, YJ Huang, V Jaravine, HRA Jonker, MA Kennedy, OF Lange, G Liu, TE Malliavin, R Mani, B Mao, GT Montelione, M Nilges, P Rossi, G Van Der Schot, H Schwalbe, TA Szyperski, M Vendruscolo, R Vernon, WF Vranken, S De Vries, GW Vuister, B Wu, Y Yang, AMJJ Bonvin
– Structure
(2012)
20,
227
(doi: 10.1016/j.str.2012.01.002)
Blind testing of routine, fully automated determination of protein structures from NMR data.
A Rosato, JM Aramini, C Arrowsmith, A Bagaria, D Baker, A Cavalli, JF Doreleijers, A Eletsky, A Giachetti, P Guerry, A Gutmanas, P Güntert, Y He, T Herrmann, YJ Huang, V Jaravine, HRA Jonker, MA Kennedy, OF Lange, G Liu, TE Malliavin, R Mani, B Mao, GT Montelione, M Nilges, P Rossi, G van der Schot, H Schwalbe, TA Szyperski, M Vendruscolo, R Vernon, WF Vranken, SD Vries, GW Vuister, B Wu, Y Yang, AMJJ Bonvin
– Structure (London, England : 1993)
(2012)
20,
227
(doi: 10.1016/j.str.2012.01.002)
Proteome folding and aggregation.
M Vendruscolo
– Curr Opin Struct Biol
(2012)
22,
138
(doi: 10.1016/j.sbi.2012.01.005)
Co-translational folding of E. coli's cytosolic proteome exhibits kinetic effects that can significantly delay folding
P Ciryam, M Vendruscolo, CM Dobson, EP O'Brien
– ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY
(2012)
244,
(link to publication)
Fibrillogenic propensity of the GroEL apical domain
J Chen, H Yagi, P Sormanni, M Vendruscolo, K Makabe, T Nakamura, Y Goto, K Kuwajima
– PROTEIN SCIENCE
(2012)
21,
102
(link to publication)
NMR chemical shifts and protein dynamics
C Camilloni, M Vendruscolo
– FEBS JOURNAL
(2012)
279,
529
(link to publication)
Protein structure validation using side-chain chemical shifts
AB Sahakyan, A Cavalli, WF Vranken, M Vendruscolo
– J Phys Chem B
(2012)
116,
4754
(doi: 10.1021/jp2122054)
Anti-oligomer monoclonal antibodies reveal that protein aggregation modulates generalized physiological and pathological disturbances
M Tayebi, M Vendruscolo, M David
– PRION
(2012)
6,
77
(link to publication)
Experimental free energy surfaces reveal the mechanisms of maintenance of protein solubility
A De Simone, A Dhulesia, G Soldi, M Vendruscolo, S-TD Hsu, F Chiti, CM Dobson
– Proc Natl Acad Sci U S A
(2011)
108,
21057
(doi: 10.1073/pnas.1112197108)
Sequence-Based Prediction of Protein Solubility
F Agostini, M Vendruscolo, GG Tartaglia
– J Mol Biol
(2011)
421,
237
(doi: 10.1016/j.jmb.2011.12.005)
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Research Groups

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Telephone number

01223 763873

Email address

mv245@cam.ac.uk

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