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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

Folding of small proteins by Monte Carlo simulations with chemical shift restraints without the use of molecular fragment replacement or structural homology.
P Robustelli, A Cavalli, CM Dobson, M Vendruscolo, X Salvatella
– Journal of Physical Chemistry B
(2009)
113,
7890
Physical principles of protein behavior in the cell
M Porto, HE Roman, M Vendruscolo
– J Proteome Res
(2009)
8,
2615
Competition between Intramolecular and Intermolecular Interactions in an Amyloid-Forming Protein
KE Routledge, GG Tartaglia, GW Platt, M Vendruscolo, SE Radford
– Journal of Molecular Biology
(2009)
389,
776
A Relationship between mRNA Expression Levels and Protein Solubility in E. coli
GG Tartaglia, S Pechmann, CM Dobson, M Vendruscolo
– J Mol Biol
(2009)
388,
381
Toward an Accurate Determination of Free Energy Landscapes in Solution States of Proteins
A De Simone, B Richter, X Salvatella, M Vendruscolo
– Journal of the American Chemical Society
(2009)
131,
3810
The mechanism of folding of Im7 reveals competition between functional and kinetic evolutionary constraints.
CT Friel, DA Smith, M Vendruscolo, J Gsponer, SE Radford
– Nature Structural & Molecular Biology
(2009)
16,
318
Factors that affect the degree of twist in beta-sheet structures: a molecular dynamics simulation study of a cross-beta filament of the GNNQQNY peptide.
X Periole, A Rampioni, M Vendruscolo, AE Mark
– Journal of Physical Chemistry B
(2009)
113,
1728
Molecular determinants of the aggregation behavior of α- and β-synuclein
RC Rivers, JR Kumita, GG Tartaglia, MM Dedmon, A Pawar, M Vendruscolo, CM Dobson, J Christodoulou
– Protein Sci
(2009)
17,
887
Similarities in the thermodynamics and kinetics of aggregation of disease-related A beta(1-40) peptides
J Meinhardt, GG Tartaglia, A Pawar, T Christopeit, P Hortschansky, V Schroeckh, CM Dobson, M Vendruscolo, M Fändrich
– Protein science : a publication of the Protein Society
(2009)
16,
1214
Competition between Folding, Native-State Dimerisation and Amyloid Aggregation in β-Lactoglobulin
D Hamada, T Tanaka, GG Tartaglia, A Pawar, M Vendruscolo, M Kawamura, A Tamura, N Tanaka, CM Dobson
– Journal of molecular biology
(2008)
386,
878
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Research Interest Groups

Telephone number

01223 763873

Email address

mv245@cam.ac.uk