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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

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
– Proceedings of the National Academy of Sciences
(2011)
108,
21057
Sequence-Based Prediction of Protein Solubility
F Agostini, M Vendruscolo, GG Tartaglia
– Journal of Molecular Biology
(2011)
421,
237
Protein solubility and protein homeostasis: A generic view of protein misfolding disorders
M Vendruscolo, TPJ Knowles, CM Dobson
– Cold Spring Harbor Perspectives in Biology
(2011)
3,
Coarse-grained model for protein folding based on structural profiles.
K Wolff, M Vendruscolo, M Porto
– Physical review. E, Statistical, nonlinear, and soft matter physics
(2011)
84,
041934
Coarse-grained model for protein folding based on structural profiles
K Wolff, M Vendruscolo, M Porto
– Physical Review E
(2011)
84,
041934
Introduction
M Buchanan, G Caldarelli, P De Los Rios, F Rao, M Vendruscolo
(2011)
17,
1
Inversion of the Balance between Hydrophobic and Hydrogen Bonding Interactions in Protein Folding and Aggregation
AW Fitzpatrick, TPJ Knowles, CA Waudby, M Vendruscolo, CM Dobson
– Plos Computational Biology
(2011)
7,
e1002169
Determination of Conformational Equilibria in Proteins Using Residual Dipolar Couplings
A De Simone, RW Montalvao, M Vendruscolo
– Journal of Chemical Theory and Computation
(2011)
7,
4189
Using Side‐Chain Aromatic Proton Chemical Shifts for a Quantitative Analysis of Protein Structures
AB Sahakyan, WF Vranken, A Cavalli, M Vendruscolo
– Angewandte Chemie (International ed. in English)
(2011)
50,
9620
Using side-chain aromatic proton chemical shifts for a quantitative analysis of protein structures
AB Sahakyan, WF Vranken, A Cavalli, M Vendruscolo
– Angewandte Chemie International Edition
(2011)
50,
9620
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Research Interest Groups

Telephone number

01223 763873

Email address

mv245@cam.ac.uk