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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

Using Side‐Chain Aromatic Proton Chemical Shifts for a Quantitative Analysis of Protein Structures
AB Sahakyan, WF Vranken, A Cavalli, M Vendruscolo
– Angew Chem Int Ed Engl
(2011)
50,
9620
(doi: 10.1002/anie.201101641)
ALS mutations in FUS cause neuronal dysfunction and death in Caenorhabditis elegans by a dominant gain-of-function mechanism.
T Murakami, S-P Yang, L Xie, T Kawano, D Fu, A Mukai, C Bohm, F Chen, J Robertson, H Suzuki, GG Tartaglia, M Vendruscolo, GS Kaminski Schierle, FTS Chan, A Moloney, D Crowther, CF Kaminski, M Zhen, P St George-Hyslop
– Hum Mol Genet
(2011)
21,
1
(doi: 10.1093/hmg/ddr417)
Excited-state control of protein activity
M Vendruscolo
– Journal of Molecular Biology
(2011)
412,
153
(doi: 10.1016/j.jmb.2011.07.047)
Nucleated polymerisation in the presence of pre-formed seed filaments
SIA Cohen, M Vendruscolo, CM Dobson, TPJ Knowles
– International journal of molecular sciences
(2011)
12,
5844
(doi: 10.3390/ijms12095844)
Nucleated Polymerisation in the Presence of Pre-Formed Seed Filaments
SIA Cohen, M Vendruscolo, CM Dobson, TPJ Knowles
– International Journal of Molecular Sciences
(2011)
12,
5844
(doi: 10.3390/ijms12095844)
Using Side‐Chain Aromatic Proton Chemical Shifts for a Quantitative Analysis of Protein Structures
AB Sahakyan, WF Vranken, A Cavalli, M Vendruscolo
– Angewandte Chemie
(2011)
123,
9794
(doi: 10.1002/ange.201101641)
On the effect of Trigger Factor on nascent chain protein folding off of the ribosome
EP O'Brien, M Vendruscolo, CM Dobson
– ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY
(2011)
242,
(link to publication)
Metastability of native proteins and the phenomenon of amyloid formation.
AJ Baldwin, TPJ Knowles, GG Tartaglia, AW Fitzpatrick, GL Devlin, SL Shammas, CA Waudby, MF Mossuto, S Meehan, SL Gras, J Christodoulou, SJ Anthony-Cahill, PD Barker, M Vendruscolo, CM Dobson
– Journal of the American Chemical Society
(2011)
133,
14160
(doi: 10.1021/ja2017703)
Nucleated polymerization with secondary pathways. II. Determination of self-consistent solutions to growth processes described by non-linear master equations.
SIA Cohen, M Vendruscolo, CM Dobson, TPJ Knowles
– The Journal of Chemical Physics
(2011)
135,
065106
(doi: 10.1063/1.3608917)
Nucleated polymerization with secondary pathways. I. Time evolution of the principal moments.
SIA Cohen, M Vendruscolo, ME Welland, CM Dobson, EM Terentjev, TPJ Knowles
– The Journal of Chemical Physics
(2011)
135,
065105
(doi: 10.1063/1.3608916)
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Research Groups

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Telephone number

01223 763873

Email address

mv245@cam.ac.uk

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