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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

An analytical solution to the kinetics of breakable filament assembly
TPJ Knowles, CA Waudby, GL Devlin, SIA Cohen, A Aguzzi, M Vendruscolo, EM Terentjev, ME Welland, CM Dobson
– Science (New York, N.Y.)
(2009)
326,
1533
(doi: 10.1126/science.1178250)
Determination of the Free Energy Landscape of alpha-Synuclein Using Spin Label Nuclear Magnetic Resonance Measurements
JR Allison, P Varnai, CM Dobson, M Vendruscolo
– Journal of the American Chemical Society
(2009)
131,
18314
(doi: 10.1021/ja904716h)
Analysis of Sub-τc and Supra-τc Motions in Protein Gβ1 Using Molecular Dynamics Simulations
JM Bui, J Gsponer, M Vendruscolo, CM Dobson
– Biophysical Journal
(2009)
97,
2513
(doi: 10.1016/j.bpj.2009.07.061)
Accurate random coil chemical shifts from an analysis of loop regions in native states of proteins.
A De Simone, A Cavalli, S-TD Hsu, W Vranken, M Vendruscolo
– J Am Chem Soc
(2009)
131,
16332
(doi: 10.1021/ja904937a)
Quantitative approaches to defining normal and aberrant protein homeostasis
M Vendruscolo, CM Dobson
– Faraday discussions
(2009)
143,
277
(doi: 10.1039/b905825g)
Fast and accurate predictions of protein NMR chemical shifts from interatomic distances.
KJ Kohlhoff, P Robustelli, A Cavalli, X Salvatella, M Vendruscolo
– J Am Chem Soc
(2009)
131,
13894
(doi: 10.1021/ja903772t)
Correlation between mRNA expression levels and protein aggregation propensities in subcellular localisations
GG Tartaglia, M Vendruscolo
– Molecular bioSystems
(2009)
5,
1873
(doi: 10.1039/b913099n)
Efficlent identification of near-native conformations in ab initio protein structure prediction using structural profiles
K Wolff, M Vendruscolo, M Porto
– Proteins
(2009)
78,
249
(doi: 10.1002/prot.22533)
Prediction of folding and misfolding of proteins from their amino acid sequences
M Vendruscolo
– ABSTR PAP AM CHEM S
(2009)
238,
(link to publication)
On the mechanism of nonspecific inhibitors of protein aggregation: Dissecting the interactions of α-synuclein with congo red and lacmoid
C Lendel, CW Bertoncini, N Cremades, CA Waudby, M Vendruscolo, CM Dobson, D Schenk, J Christodoulou, G Toth
– Biochemistry
(2009)
48,
8322
(doi: 10.1021/bi901285x)
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Telephone number

01223 763873

Email address

mv245@cam.ac.uk

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