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Yusuf Hamied Department of Chemistry

 

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

Networks in cell biology
M Buchanan, G Caldarelli, P De Los Rios, F Rao, M Vendruscolo
(2010)
i
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
(2009)
326,
1533
Determination of the Free Energy Landscape of α-Synuclein Using Spin Label Nuclear Magnetic Resonance Measurements
JR Allison, P Varnai, CM Dobson, M Vendruscolo
– J Am Chem Soc
(2009)
131,
18314
Analysis of sub-τc and supra-τc motions in protein Gβ1 using molecular dynamics simulations
JM Bui, J Gsponer, M Vendruscolo, CM Dobson
– Biophys J
(2009)
97,
2513
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
– Journal of the American Chemical Society
(2009)
131,
16332
Quantitative approaches to defining normal and aberrant protein homeostasis
M Vendruscolo, CM Dobson
– Faraday Discuss
(2009)
143,
277
Fast and accurate predictions of protein NMR chemical shifts from interatomic distances
KJ Kohlhoff, P Robustelli, A Cavalli, X Salvatella, M Vendruscolo
– Journal of the American Chemical Society
(2009)
131,
13894
Correlation between mRNA expression levels and protein aggregation propensities in subcellular localisations
GG Tartaglia, M Vendruscolo
– Mol Biosyst
(2009)
5,
1873
Efficient identification of near-native conformations in ab initio protein structure prediction using structural profiles
K Wolff, M Vendruscolo, M Porto
– Proteins: Structure, Function, and Bioinformatics
(2009)
78,
249
Prediction of folding and misfolding of proteins from their amino acid sequences
M Vendruscolo
– ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY
(2009)
238,
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Research Interest Groups

Telephone number

01223 763873

Email address

mv245@cam.ac.uk