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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

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
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
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,
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
– J Am Chem Soc
(2011)
133,
14160
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
– J Chem Phys
(2011)
135,
065106
Nucleated polymerization with secondary pathways. I. Time evolution of the principal moments
SIA Cohen, M Vendruscolo, ME Welland, CM Dobson, EM Terentjev, TPJ Knowles
– Journal of Chemical Physics
(2011)
135,
065105
Nucleated polymerization with secondary pathways. III. Equilibrium behavior and oligomer populations
SIA Cohen, M Vendruscolo, CM Dobson, TPJ Knowles
– J Chem Phys
(2011)
135,
065107
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,
a010454
The A53T Mutation is Key in Defining the Differences in the Aggregation Kinetics of Human and Mouse alpha-Synuclein
L Kang, K-P Wu, M Vendruscolo, J Baum
– Journal of the American Chemical Society
(2011)
133,
13465
Structure-Based Prediction of Methyl Chemical Shifts in Proteins.
AB Sahakyan, WF Vranken, A Cavalli, M Vendruscolo
– Journal of Biomolecular NMR
(2011)
50,
1
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Research Interest Groups

Telephone number

01223 763873

Email address

mv245@cam.ac.uk